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3OUU

Crystal Structure of Biotin Carboxylase-beta-gamma-ATP Complex from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
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
B0003989molecular_functionacetyl-CoA carboxylase activity
B0004075molecular_functionbiotin carboxylase activity
B0005524molecular_functionATP binding
B0006633biological_processfatty acid biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
B2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 452
ChainResidue
ATYR33
ALYS38

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 457
ChainResidue
ATRP183
ASER184
AHOH572
AHOH612
BPHE347
BPRO349

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 458
ChainResidue
AASN291
AANP460
AHOH588
AGLU289

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 459
ChainResidue
AGLU276
AGLU289
AANP460
AHOH478

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ANP A 460
ChainResidue
ALYS117
AILE132
AILE157
ALYS159
AGLY164
AGLY165
AGLY166
AMSE169
AGLU201
ALYS202
ATYR203
AILE204
AHIS209
AGLN233
AHIS236
AGLU276
ALEU278
AGLU289
ATHR437
ACA458
ACA459
AHOH531
AHOH603
AHOH715

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CAC A 461
ChainResidue
AMSE114
ASER115
ALYS117
AALA161
AALA162
AGLY163
AHOH533
AHOH561
AHOH588
AHOH730
AHOH732

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 453
ChainResidue
AASP39
ATYR372
AHOH648
BLYS356
BILE358

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 454
ChainResidue
BLYS38
BHOH570

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 455
ChainResidue
BGLU276
BGLU289
BANP457
BHOH610

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 456
ChainResidue
BGLU289
BASN291
BANP457
BHOH611
BHOH684

site_idBC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ANP B 457
ChainResidue
BLYS117
BILE132
BILE157
BLYS159
BGLY164
BGLY165
BGLY166
BMSE169
BGLU201
BLYS202
BTYR203
BILE204
BHIS209
BGLN233
BHIS236
BGLU276
BLEU278
BGLU289
BTHR437
BHOH444
BCA455
BCA456
BHOH508
BHOH583
BHOH584
BHOH585
BHOH610
BHOH615
BHOH717
BHOH736

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CAC B 458
ChainResidue
BLYS117
BALA161
BALA162
BGLY163
BHOH560
BHOH612
BHOH684
BMSE114
BSER115

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 459
ChainResidue
BSER344
BLYS415
BTHR416

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

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRL
ChainResidueDetails
APHE287-LEU294

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PDB entries from 2024-11-06

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