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7OJ2

Bacillus subtilis IMPDH in complex with Ap4A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue PO4 A 501
ChainResidue
AGLY305
AHOH698
AHOH704
ASER306
AGLY342
AGLY343
AGLY364
ASER365
ATYR388
AHOH631
AHOH636

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 502
ChainResidue
ATHR37
ATHR39
AGLU273
ALEU274
AASN275
AASP296
ALYS336
AHOH635
AHOH665
AHOH714

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 503
ChainResidue
ALYS38
AARG332
AHIS359
AARG452
AARG455
AHOH664
AHOH728

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL298-THR310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
ACYS308

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AARG404

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AASP251
AHIS472
AGLY301
ASER306
AASP341
AGLY364
ATYR388
AGLU416
AGLU470
ASER471

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AGLY303
AGLY305
ACYS308

226707

PDB entries from 2024-10-30

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