Magnesium in PDB 2jih: Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)

The structure of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form), PDB code: 2jih was solved by S.Gerhardt, G.Hassall, P.Hawtin, E.Mccall, L.Flavell, C.Minshull, D.Hargreaves, A.Ting, R.A.Pauptit, A.E.Parker, W.M.Abbott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.90 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.579, 64.396, 113.524, 90.00, 90.91, 90.00
R / Rfree (%)	22.4 / 28.2

The structure of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) also contains other interesting chemical elements:

Nickel	(Ni)	12 atoms
Zinc	(Zn)	2 atoms
Cadmium	(Cd)	6 atoms
Sodium	(Na)	5 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) (pdb code 2jih). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form), PDB code: 2jih:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1560 b:35.8 occ:1.00 O A:HOH2035 2.3 40.8 1.0 ND1 A:HIS339 3.0 42.8 1.0 CE1 A:HIS339 3.8 45.7 1.0 CG A:HIS339 3.9 43.6 1.0 CB A:HIS339 4.2 43.4 1.0 CA A:HIS339 4.2 43.0 1.0 NZ A:LYS308 4.3 43.1 1.0 CE A:LYS308 4.6 43.8 1.0 O A:HIS339 4.6 42.1 1.0 C A:HIS339 4.9 42.6 1.0 O A:GLN338 4.9 43.5 1.0 NE2 A:HIS339 4.9 45.2 1.0 CD1 A:LEU310 4.9 38.8 1.0 CD2 A:HIS339 5.0 43.9 1.0

Magnesium binding site 2 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1569 b:26.4 occ:1.00 CB A:LEU519 2.9 48.9 1.0 N A:LEU519 3.1 49.7 1.0 CA A:LEU519 3.6 49.0 1.0 CG2 A:VAL518 3.6 51.5 1.0 CG A:LEU519 4.2 50.4 1.0 C A:VAL518 4.2 50.4 1.0 CD2 A:LEU519 4.2 51.8 1.0 CA A:VAL518 4.4 50.8 1.0 CB A:VAL518 4.6 50.9 1.0 C A:LEU519 4.9 47.6 1.0

Magnesium binding site 3 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1560 b:55.3 occ:1.00 OD1 B:ASN542 2.3 45.5 1.0 OD2 B:ASP530 2.7 31.5 1.0 ND1 B:HIS439 3.2 43.5 1.0 CE1 B:HIS439 3.3 45.8 1.0 OD1 B:ASP530 3.4 34.3 1.0 CG B:ASP530 3.4 32.5 1.0 CG B:ASN542 3.4 42.0 1.0 CA B:ASN542 3.9 39.5 1.0 N B:ASN542 4.1 39.5 1.0 O B:HOH2079 4.2 37.5 1.0 CB B:ASN542 4.2 39.7 1.0 CG B:HIS439 4.3 44.9 1.0 NE2 B:HIS439 4.4 45.8 1.0 ND2 B:ASN542 4.5 43.7 1.0 CD2 B:HIS439 4.9 46.2 1.0 CB B:ASP530 4.9 33.1 1.0 CZ B:PHE397 4.9 43.1 1.0

Magnesium binding site 4 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1562 b:41.0 occ:1.00 NE2 B:HIS459 2.5 35.9 1.0 CD2 B:HIS459 3.3 37.0 1.0 CE1 B:HIS459 3.5 36.3 1.0 O B:HOH2057 3.8 35.9 1.0 CB B:ASN457 4.2 33.2 1.0 CG B:HIS459 4.5 35.3 1.0 CG B:ASN457 4.6 32.0 1.0 ND1 B:HIS459 4.6 37.6 1.0 OD1 B:ASN457 4.9 32.7 1.0

Magnesium binding site 5 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1566 b:30.9 occ:1.00 ND1 B:HIS339 2.5 48.1 1.0 CE1 B:HIS339 3.4 47.0 1.0 CG B:HIS339 3.5 47.3 1.0 CB B:HIS339 3.7 47.4 1.0 CA B:HIS339 3.9 47.1 1.0 NZ B:LYS308 4.1 44.2 1.0 NE2 B:HIS339 4.5 47.4 1.0 O B:HIS339 4.6 47.0 1.0 CD2 B:HIS339 4.6 47.2 1.0 CE B:LYS308 4.6 43.0 1.0 O B:GLN338 4.7 46.6 1.0 C B:HIS339 4.8 47.1 1.0 N B:HIS339 4.9 46.9 1.0

Magnesium binding site 6 out of 6 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1567 b:20.6 occ:1.00 NE2 B:HIS439 2.4 45.8 1.0 CD2 B:HIS439 3.4 46.2 1.0 CE1 B:HIS439 3.4 45.8 1.0 O B:LEU437 3.9 49.6 1.0 O B:ASN542 4.3 39.1 1.0 C B:ASN542 4.5 39.0 1.0 N B:LEU437 4.5 49.2 1.0 ND1 B:HIS439 4.5 43.5 1.0 CG B:HIS439 4.5 44.9 1.0 C B:LEU437 4.9 48.9 1.0 CA B:ASN542 5.0 39.5 1.0 CB B:ASN436 5.0 50.0 1.0 CA B:ASN436 5.0 50.1 1.0 C B:ASN436 5.0 49.8 1.0

S.Gerhardt, G.Hassall, P.Hawtin, E.Mccall, L.Flavell, C.Minshull, D.Hargreaves, A.Ting, R.A.Pauptit, A.E.Parker, W.M.Abbott. Crystal Structures of Human Adamts-1 Reveal A Conserved Catalytic Domain and A Disintegrin-Like Domain with A Fold Homologous to Cysteine-Rich Domains. J. Mol. Biol. V. 373 891 2007.
ISSN: ISSN 0022-2836
PubMed: 17897672
DOI: 10.1016/J.JMB.2007.07.047