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4MV7

Crystal Structure of Biotin Carboxylase form Haemophilus influenzae in Complex with Phosphonoformate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005524molecular_functionATP binding
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
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 Residues12
DetailsBINDING SITE FOR RESIDUE PPF A 501
ChainResidue
ALYS238
AHOH664
AHOH753
AHOH766
AASN290
AARG292
AGLN294
AVAL295
AGLU296
AARG338
AHOH627
AHOH643

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AMET1
ALEU2

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
ASER359
ASER359
APRO360
APRO360
AGLY361
ATRP367
ATRP367
AHOH634

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

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI
ChainResidueDetails
APHE286-ILE293

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 Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV8
ChainResidueDetails
ALYS116

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4
ChainResidueDetails
ALYS159

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P24182
ChainResidueDetails
AGLY165
AHIS209
AHIS236
ALYS238
AARG292
AVAL295
AARG338

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV8, ECO:0007744|PDB:4RZQ
ChainResidueDetails
AGLU201

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
ChainResidueDetails
AGLU276
AGLU288
AASN290

217705

数据于2024-03-27公开中

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