Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8JXL

Human 3-methylcrotonyl-CoA carboxylase in MCCU state with MCoA

Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GDsLmvMiAMKMehtIkS
ChainResidueDetails
FGLY671-SER688

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FMEMNTRL
ChainResidueDetails
FPHE333-LEU340

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P24182
ChainResidueDetails
FARG339
ILYS495
KLYS70
KLYS495
CARG339
EARG339
HARG339
JARG339
LARG339
GLYS70
GLYS495
ILYS70

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P24182
ChainResidueDetails
FLYS163
CHIS255
CHIS282
CGLU322
ELYS163
ELYS205
EGLY211
EHIS255
EHIS282
EGLU322
HLYS163
FLYS205
HLYS205
HGLY211
HHIS255
HHIS282
HGLU322
JLYS163
JLYS205
JGLY211
JHIS255
JHIS282
FGLY211
JGLU322
LLYS163
LLYS205
LGLY211
LHIS255
LHIS282
LGLU322
FHIS255
FHIS282
FGLU322
CLYS163
CLYS205
CGLY211

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99MR8
ChainResidueDetails
FLYS237
JLYS494
LLYS237
LLYS494
FLYS494
CLYS237
CLYS494
ELYS237
ELYS494
HLYS237
HLYS494
JLYS237

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99MR8
ChainResidueDetails
FLYS581
CLYS581
ELYS581
HLYS581
JLYS581
LLYS581

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-biotinyllysine => ECO:0000255|PROSITE-ProRule:PRU01066
ChainResidueDetails
FLYS681
CLYS681
ELYS681
HLYS681
JLYS681
LLYS681

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon