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3GID

The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2) in complex with Soraphen A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0005524molecular_functionATP binding
A0046872molecular_functionmetal ion binding
B0003989molecular_functionacetyl-CoA carboxylase activity
B0005524molecular_functionATP binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE S1A A 1000
ChainResidue
ALYS274
APHE704
ATRP706
AARG277
ASER278
AARG281
AGLU593
AMET594
AASN599
AASN679
ATRP681

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE S1A B 1000
ChainResidue
BLYS274
BARG277
BSER278
BARG281
BGLU593
BMET594
BVAL598
BASN599
BASN679
BTRP681
BPHE704
BSER705
BTRP706

Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPLMIKASeggGGkG
ChainResidueDetails
APHE449-GLY463

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL
ChainResidueDetails
APHE578-LEU585

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG584
BARG584

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
ChainResidueDetails
AGLY458
BGLY458

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969
ChainResidueDetails
AGLU567
AASN582
BGLU567
BGLU580
BASN582
AGLU580

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER469
BSER469

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q13085
ChainResidueDetails
ATHR753
BTHR753

219869

PDB entries from 2024-05-15

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