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6OJH

Crystal Structure of Haemophilus Influenzae Biotin Carboxylase Complexed with (R)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine

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 Residues12
Detailsbinding site for residue MV4 A 501
ChainResidue
AILE157
AGLU288
AILE437
AHOH658
ALYS159
AMET169
AGLU201
ALYS202
ATYR203
ALEU204
AHIS236
ALEU278

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 502
ChainResidue
AGLU276
AGLU288
AASN290
AACT503
AHOH695

site_idAC3
Number of Residues7
Detailsbinding site for residue ACT A 503
ChainResidue
AGLU276
AGLU288
AASN290
AARG292
ACA502
AHOH610
AHOH658

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

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PDB entries from 2024-07-17

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