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7KQ4

Structure of isethionate sulfite-lyase from Bilophila wadsworthia with glycerol 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
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 901
ChainResidue
AARG189
AILE192
AGLN193
ATYR587
AARG678
APHE682
AHOH1007
AHOH1088

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL B 901
ChainResidue
BILE192
BGLN193
BGLU470
BTYR587
BARG678
BHOH1026
BHOH1147
BARG189

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 Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000250|UniProtKB:Q30W70
ChainResidueDetails
BCYS468
ACYS468

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q30W70
ChainResidueDetails
BGLU470
AGLU470

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q727N1
ChainResidueDetails
BCYS468
BARG678
AARG678
BARG189
BGLN193
AARG189
AGLN193
ACYS468

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Glycine radical => ECO:0000255|PROSITE-ProRule:PRU00493
ChainResidueDetails
BGLY805
AGLY805

221051

PDB entries from 2024-06-12

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