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2A3L

X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003876molecular_functionAMP deaminase activity
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0019239molecular_functiondeaminase activity
A0032264biological_processIMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 840
ChainResidue
AHIS391
AHIS393
AHIS659
AASP736
ACF5841

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 842
ChainResidue
AARG380
AARG386

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CF5 A 841
ChainResidue
AHIS393
ALYS462
APHE463
ALYS466
ATYR467
AHIS659
AGLU662
AHIS681
ASER708
AASP736
AASP737
AGLN740
AZN840
AILE220
AHIS391

Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLSTDDP
ChainResidueDetails
ASER732-PRO738

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AHIS681

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AALA289

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AHIS391
AHIS393
ALYS462
AHIS659
AGLU662
AASP736
AASP737

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18433157
ChainResidueDetails
ASER140
ASER203

222415

PDB entries from 2024-07-10

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