Magnesium in PDB 8swn: Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc

The binding sites of Magnesium atom in the Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc (pdb code 8swn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc, PDB code: 8swn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1401 b:64.6 occ:1.00 O2B A:ATP1404 1.9 54.7 1.0 OG A:SER1082 2.0 65.0 1.0 O1G A:ATP1404 2.0 61.1 1.0 OE1 A:GLN1122 2.1 53.7 1.0 HG A:SER1082 2.4 56.0 1.0 HE22 A:GLN1202 2.8 66.5 1.0 HE22 A:GLN1122 3.0 57.5 1.0 CD A:GLN1122 3.0 50.8 1.0 CB A:SER1082 3.1 53.8 1.0 HB2 A:SER1082 3.1 55.5 1.0 H A:SER1082 3.3 56.1 1.0 PG A:ATP1404 3.3 65.2 1.0 PB A:ATP1404 3.4 38.9 1.0 NE2 A:GLN1122 3.4 56.4 1.0 NE2 A:GLN1202 3.4 65.4 1.0 HE21 A:GLN1202 3.5 65.8 1.0 O1A A:ATP1404 3.6 48.2 1.0 HB3 A:SER1082 3.7 54.3 1.0 O3B A:ATP1404 3.8 58.7 1.0 OD2 A:ASP1201 3.9 73.9 1.0 N A:SER1082 3.9 51.9 1.0 H A:GLY537 4.0 53.0 1.0 CA A:SER1082 4.1 45.3 1.0 HB2 A:SER536 4.1 50.6 1.0 OD1 A:ASP1201 4.2 78.0 1.0 O1B A:ATP1404 4.2 50.1 1.0 HE21 A:GLN1122 4.2 56.4 1.0 HB2 A:LYS1081 4.2 61.8 1.0 O3G A:ATP1404 4.2 50.6 1.0 HB2 A:GLN1122 4.2 56.7 1.0 CG A:GLN1122 4.4 50.1 1.0 O2G A:ATP1404 4.4 54.6 1.0 O3A A:ATP1404 4.4 49.0 1.0 PA A:ATP1404 4.4 43.1 1.0 HA A:SER1082 4.5 53.8 1.0 CG A:ASP1201 4.5 72.8 1.0 HE2 A:LYS1081 4.5 63.3 1.0 HG21 A:ILE1231 4.6 65.0 1.0 CD A:GLN1202 4.6 74.0 1.0 CB A:GLN1122 4.7 57.0 1.0 HG3 A:GLN1122 4.8 55.9 1.0 HB3 A:GLN1122 4.8 57.1 1.0 HD11 A:ILE1231 4.8 63.9 1.0 HA A:SER536 4.8 51.2 1.0 N A:GLY537 4.9 51.0 1.0 O2A A:ATP1404 4.9 62.5 1.0 HZ3 A:LYS1081 4.9 62.8 1.0 CB A:SER536 5.0 48.0 1.0 OE1 A:GLN1202 5.0 75.5 1.0

Magnesium binding site 2 out of 2 in the Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bovine Multidrug Resistance Protein 4 (MRP4) E1202Q Mutant Bound to Atp in Msp Lipid Nanodisc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1402 b:53.7 occ:1.00 O3G A:ATP1405 1.8 59.6 1.0 OG A:SER452 1.9 55.0 1.0 O2B A:ATP1405 1.9 55.0 1.0 OE1 A:GLN480 2.0 62.0 1.0 HG A:SER452 2.4 51.0 1.0 CD A:GLN480 2.9 61.4 1.0 HB2 A:SER452 3.0 51.7 1.0 CB A:SER452 3.0 46.3 1.0 HE22 A:GLN480 3.0 57.7 1.0 H A:SER452 3.2 51.4 1.0 PG A:ATP1405 3.3 54.5 1.0 NE2 A:GLN480 3.3 62.4 1.0 PB A:ATP1405 3.3 48.2 1.0 HB3 A:SER452 3.6 49.2 1.0 O3B A:ATP1405 3.8 56.1 1.0 N A:SER452 3.8 40.7 1.0 OD1 A:ASP559 3.9 54.0 1.0 CA A:SER452 4.0 36.3 1.0 O1A A:ATP1405 4.0 44.5 1.0 HB2 A:SER1178 4.0 54.1 1.0 O2G A:ATP1405 4.1 57.3 1.0 HB2 A:GLN480 4.1 57.6 1.0 H A:VAL1179 4.1 57.9 1.0 O1B A:ATP1405 4.1 50.9 1.0 OD2 A:ASP559 4.1 62.9 1.0 HE21 A:GLN480 4.2 57.4 1.0 O1G A:ATP1405 4.3 49.2 1.0 CG A:GLN480 4.3 57.7 1.0 HG21 A:VAL1179 4.3 57.3 1.0 HA A:SER452 4.3 49.0 1.0 HB2 A:LYS451 4.3 57.3 1.0 CG A:ASP559 4.4 58.5 1.0 O3A A:ATP1405 4.5 61.1 1.0 HG11 A:VAL590 4.5 58.2 1.0 CB A:GLN480 4.6 59.5 1.0 HB A:VAL1179 4.6 57.1 1.0 HB3 A:GLN480 4.6 56.6 1.0 PA A:ATP1405 4.7 42.0 1.0 HE2 A:LYS451 4.8 57.2 1.0 HG3 A:GLN480 4.8 57.3 1.0 HG2 A:GLN480 4.8 56.4 1.0 CB A:SER1178 5.0 49.8 1.0 N A:VAL1179 5.0 54.5 1.0 C A:LYS451 5.0 47.0 1.0

S.Pourmal, E.Green, R.Bajaj, I.E.Chemmama, G.M.Knudsen, M.Gupta, A.Sali, Y.Cheng, C.S.Craik, D.L.Kroetz, R.M.Stroud. Structural Basis of Prostaglandin Efflux By MRP4. Nat.Struct.Mol.Biol. 2024.
ISSN: ESSN 1545-9985
PubMed: 38216659
DOI: 10.1038/S41594-023-01176-4