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3RV4

Crystal structure of E.coli biotin carboxylase R16E mutant in complex with Mg-ADP and bicarbonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
A0016874molecular_functionligase activity
A0042803molecular_functionprotein homodimerization activity
A0045717biological_processnegative regulation of fatty acid biosynthetic process
A0046872molecular_functionmetal ion binding
A2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 1000
ChainResidue
ALYS116
ATYR203
ALEU204
AHIS209
AGLN233
AHIS236
AGLU276
ALEU278
AILE287
AGLU288
AILE437
AILE157
AHOH551
AHOH813
AMG1004
AGOL1014
ALYS159
AGLY164
AGLY165
AGLY166
AMET169
AGLU201
ALYS202

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1004
ChainResidue
AGLU276
AGLU288
AHOH551
AHOH673
AADP1000

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BCT A 1006
ChainResidue
ALYS238
AARG292
AGLN294
AVAL295
AGLU296
AARG338
AHOH536

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CS A 1008
ChainResidue
AMET113
AGLU288
AMET289
AHOH547
AHOH596

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1010
ChainResidue
AASN345
APHE347
AASN429
AGLY433

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1012
ChainResidue
AGLN407
ALEU409
AHOH470

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1014
ChainResidue
ATYR203
AGLN233
AARG235
AHIS236
AILE437
AHIS438
AGLU441
AHOH707
AADP1000

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 450
ChainResidue
AVAL377
APRO378
AASP382
AHOH671

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 451
ChainResidue
AHIS79
AGLY81
AILE293
AGLN312
AHOH478

Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG
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:0000269|PubMed:19213731
ChainResidueDetails
AARG292

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D
ChainResidueDetails
ALYS116
AGLY165

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
ChainResidueDetails
ALYS159

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
ChainResidueDetails
AGLU201

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
ChainResidueDetails
AHIS209
ALYS238
AARG292
AVAL295
AARG338

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C
ChainResidueDetails
AHIS236

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
ChainResidueDetails
AGLU276
AGLU288
AASN290

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PDB entries from 2024-08-07

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