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9WKR

structure of human propionyl-coenzyme A carboxylase in BC binding state

Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GQeIcvIeAMKMqnsMtA
ChainResidueDetails
AGLY684-ALA701

site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASaggGGkG
ChainResidueDetails
ATYR214-GLY228

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEMNTRL
ChainResidueDetails
APHE347-LEU354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2682
DetailsDomain: {"description":"Biotin carboxylation","evidences":[{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1182
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues450
DetailsDomain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues384
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q5LUF3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91ZA3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91ZA3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q91ZA3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91ZA3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsModified residue: {"description":"N6-biotinyllysine; by HLCS","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20443544","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1434
DetailsDomain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues198
DetailsRegion: {"description":"Acyl-CoA binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues18
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99MN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99MN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

260320

PDB entries from 2026-09-30

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