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2VQD

Crystal Structure of Biotin Carboxylase from Pseudomonas aeruginosa complexed with AMPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005524molecular_functionATP binding
A0006633biological_processfatty acid biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
A2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE AP2 A1448
ChainResidue
ALYS116
ALYS202
APHE203
ALEU204
AHIS209
AGLN233
AHIS236
AGLU276
ALEU278
AGLU288
AILE437
AILE157
AMG1449
AHOH2092
AHOH2231
ALYS159
AGLY163
AGLY164
AGLY165
AGLY166
AMET169
AGLU201

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A1449
ChainResidue
AGLU276
AGLU288
AAP21448
AHOH2133
AHOH2139

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1450
ChainResidue
AGLU87
AMET113
AGLY114
AGLY163
AGLU288
AMET289
AHOH2140

Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKAAgggGGrG
ChainResidueDetails
ATYR154-GLY168

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRV
ChainResidueDetails
APHE286-VAL293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P24182
ChainResidueDetails
AARG292

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P24182
ChainResidueDetails
ALYS116
AARG338
ALYS159
AGLY165
AGLU201
AHIS209
AHIS236
ALYS238
AARG292
AVAL295

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
ChainResidueDetails
AGLU276
AGLU288
AASN290

220113

PDB entries from 2024-05-22

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