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Magnesium in PDB 1vfv: Crystal Structure of the KIF1A Motor Domain Complexed with Mg-Amppnp

Protein crystallography data

The structure of Crystal Structure of the KIF1A Motor Domain Complexed with Mg-Amppnp, PDB code: 1vfv was solved by R.Nitta, M.Kikkawa, Y.Okada, N.Hirokawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.17 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.584, 55.233, 157.056, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 24.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the KIF1A Motor Domain Complexed with Mg-Amppnp (pdb code 1vfv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the KIF1A Motor Domain Complexed with Mg-Amppnp, PDB code: 1vfv:

Magnesium binding site 1 out of 1 in 1vfv

Go back to Magnesium Binding Sites List in 1vfv
Magnesium binding site 1 out of 1 in the Crystal Structure of the KIF1A Motor Domain Complexed with Mg-Amppnp


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 the KIF1A Motor Domain Complexed with Mg-Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:36.6
occ:1.00
OG A:SER104 2.1 20.9 1.0
O2G A:ANP500 2.3 32.1 1.0
O A:HOH503 2.4 32.9 1.0
O1B A:ANP500 2.4 21.5 1.0
O A:HOH504 2.4 26.2 1.0
O A:HOH502 2.5 39.5 1.0
CB A:SER104 3.2 23.8 1.0
PB A:ANP500 3.3 25.3 1.0
PG A:ANP500 3.5 34.1 1.0
N3B A:ANP500 3.5 24.7 1.0
N A:SER104 3.8 19.4 1.0
O A:HOH539 3.8 45.9 1.0
OD2 A:ASP248 4.0 24.7 1.0
CA A:SER104 4.0 18.5 1.0
O3A A:ANP500 4.2 20.5 1.0
OD1 A:ASP248 4.2 24.3 1.0
O A:HOH580 4.2 43.8 1.0
O A:HOH602 4.3 36.4 1.0
OG A:SER215 4.3 51.5 1.0
PA A:ANP500 4.3 32.8 1.0
O3G A:ANP500 4.3 38.4 1.0
O1G A:ANP500 4.5 38.8 1.0
CG A:ASP248 4.5 27.0 1.0
CE A:LYS103 4.6 21.7 1.0
O1A A:ANP500 4.7 31.0 1.0
O2B A:ANP500 4.7 28.0 1.0
O A:LEU249 4.7 22.7 1.0
CB A:LYS103 4.7 18.6 1.0
CB A:SER215 4.9 61.6 1.0
C A:LYS103 4.9 21.6 1.0
NZ A:LYS103 5.0 26.3 1.0

Reference:

R.Nitta, M.Kikkawa, Y.Okada, N.Hirokawa. KIF1A Alternately Uses Two Loops to Bind Microtubules Science V. 305 678 2004.
ISSN: ISSN 0036-8075
PubMed: 15286375
DOI: 10.1126/SCIENCE.1096621
Page generated: Tue Aug 13 15:03:31 2024

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