Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MQW

Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006753biological_processnucleoside phosphate metabolic process
A0019693biological_processribose phosphate metabolic process
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AALA76
AGLU97
AADV301
AMN402
AHOH406
AHOH412

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AADV301
AMN401
AHOH407
AGLU93
AGLU97
AGLU142

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 403
ChainResidue
AARG92
AGLU93
AADV301
AHOH404
AHOH405
AHOH407

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ADV A 301
ChainResidue
AARG37
AGLN62
AARG64
AALA76
AGLY77
ALEU78
AGLU93
AGLU97
AGLY116
AHIS139
AHIS140
AGLU142
AMN401
AMN402
AMN403
AHOH404
AHOH406
AHOH407
AHOH410
AHOH412
AHOH413

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12906832, 12135348
ChainResidueDetails
AGLU142
AARG64

site_idMCSA1
Number of Residues5
DetailsM-CSA 823
ChainResidueDetails
AARG64electrostatic stabiliser
AALA76metal ligand
AGLU93metal ligand
AGLU97metal ligand
AGLU142metal ligand, proton acceptor

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon