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

2IDB

Crystal Structure of 3-octaprenyl-4-hydroxybenzoate decarboxylase (UbiD) from Escherichia coli, Northeast Structural Genomics Target ER459.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006744biological_processubiquinone biosynthetic process
A0008694molecular_function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0030145molecular_functionmanganese ion binding
A0032150biological_processubiquinone biosynthetic process from chorismate
A0034214biological_processprotein hexamerization
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0120233molecular_functionprenyl-FMNH2 binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006744biological_processubiquinone biosynthetic process
B0008694molecular_function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
B0016831molecular_functioncarboxy-lyase activity
B0030145molecular_functionmanganese ion binding
B0032150biological_processubiquinone biosynthetic process from chorismate
B0034214biological_processprotein hexamerization
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0120233molecular_functionprenyl-FMNH2 binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006744biological_processubiquinone biosynthetic process
C0008694molecular_function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
C0016831molecular_functioncarboxy-lyase activity
C0030145molecular_functionmanganese ion binding
C0032150biological_processubiquinone biosynthetic process from chorismate
C0034214biological_processprotein hexamerization
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0120233molecular_functionprenyl-FMNH2 binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 506
ChainResidue
ATHR160
ATRP161
AHIS291
ATHR320
APRO329

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AGLY468
AHOH570

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE B 506
ChainResidue
BGLY468
BTRP459
BTRP467

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 1PE C 506
ChainResidue
CTRP459
CTRP467

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 508
ChainResidue
CASP403
CASP404

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000305|PubMed:28057757
ChainResidueDetails
AASP290
BASP290
CASP290

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:28057757, ECO:0007744|PDB:5M1D, ECO:0007744|PDB:5M1E
ChainResidueDetails
AASN175
BGLU241
CASN175
CILE178
CARG192
CARG197
CGLU241
AILE178
AARG192
AARG197
AGLU241
BASN175
BILE178
BARG192
BARG197

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon