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7KQ3

Structure of isethionate sulfite-lyase from Bilophila wadsworthia with substrate isethionate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0016829molecular_functionlyase activity
A0046306biological_processalkanesulfonate catabolic process
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0016829molecular_functionlyase activity
B0046306biological_processalkanesulfonate catabolic process
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0016829molecular_functionlyase activity
C0046306biological_processalkanesulfonate catabolic process
D0003824molecular_functioncatalytic activity
D0005829cellular_componentcytosol
D0016829molecular_functionlyase activity
D0046306biological_processalkanesulfonate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 8X3 A 901
ChainResidue
AARG189
APHE682
AHOH1112
AILE192
AGLN193
ATHR312
ASER466
AGLY467
ACYS468
AGLU470
AARG678

site_idAC2
Number of Residues11
Detailsbinding site for residue 8X3 B 901
ChainResidue
BARG189
BILE192
BGLN193
BTHR312
BGLY467
BCYS468
BGLU470
BTYR587
BARG678
BPHE682
BHOH1088

site_idAC3
Number of Residues11
Detailsbinding site for residue 8X3 C 901
ChainResidue
CARG189
CILE192
CGLN193
CTHR312
CSER466
CGLY467
CCYS468
CGLU470
CARG678
CPHE682
CHOH1115

site_idAC4
Number of Residues10
Detailsbinding site for residue 8X3 D 901
ChainResidue
DARG189
DILE192
DGLN193
DTHR312
DGLY467
DCYS468
DGLU470
DARG678
DPHE682
DHOH1073

Functional Information from PROSITE/UniProt
site_idPS00850
Number of Residues9
DetailsGLY_RADICAL_1 Glycine radical domain signature. IvRIAGYSA
ChainResidueDetails
AILE800-ALA808

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000250|UniProtKB:Q30W70
ChainResidueDetails
BCYS468
CCYS468
DCYS468
ACYS468

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q30W70
ChainResidueDetails
BGLU470
CGLU470
DGLU470
AGLU470

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q727N1
ChainResidueDetails
DARG189
DGLN193
DCYS468
DARG678
AARG678
BARG189
BGLN193
BCYS468
BARG678
CARG189
CGLN193
CCYS468
CARG678
AARG189
AGLN193
ACYS468

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Glycine radical => ECO:0000255|PROSITE-ProRule:PRU00493
ChainResidueDetails
BGLY805
CGLY805
DGLY805
AGLY805

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PDB entries from 2024-06-12

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