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

5YMR

The Crystal Structure of IseG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0046306biological_processalkanesulfonate catabolic process
B0003824molecular_functioncatalytic activity
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0046306biological_processalkanesulfonate catabolic process
C0003824molecular_functioncatalytic activity
C0016740molecular_functiontransferase activity
C0016829molecular_functionlyase activity
C0046306biological_processalkanesulfonate catabolic process
D0003824molecular_functioncatalytic activity
D0016740molecular_functiontransferase activity
D0016829molecular_functionlyase activity
D0046306biological_processalkanesulfonate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 8X3 B 901
ChainResidue
BARG187
BHOH1124
BILE190
BGLN191
BTHR310
BGLY465
BCYS466
BGLU468
BARG676
BPHE680

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL B 902
ChainResidue
BARG31
BHIS88
BLEU90
BGLU269
BGLU341

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL B 903
ChainResidue
APHE726
BARG385
BASP386
BARG416

site_idAC4
Number of Residues11
Detailsbinding site for residue 8X3 D 901
ChainResidue
DARG187
DILE190
DGLN191
DTHR310
DGLY465
DCYS466
DGLU468
DTYR585
DARG676
DPHE680
DHOH1038

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL D 902
ChainResidue
CPHE726
DARG416

site_idAC6
Number of Residues11
Detailsbinding site for residue 8X3 C 901
ChainResidue
CARG187
CILE190
CGLN191
CTHR310
CGLY465
CCYS466
CGLU468
CTYR585
CARG676
CPHE680
CHOH1121

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL C 902
ChainResidue
CASP386
CARG416
DGLN723
DPHE726

site_idAC8
Number of Residues10
Detailsbinding site for residue 8X3 A 901
ChainResidue
AARG187
AILE190
AGLN191
ATHR310
AGLY465
ACYS466
AGLU468
AARG676
APHE680
AHOH1133

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL A 902
ChainResidue
AARG31
AHIS88
ALEU90
AGLU269
AGLU341

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 903
ChainResidue
AMET58
ALEU66
AARG69
ALYS149
AARG551
AHIS552

Functional Information from PROSITE/UniProt
site_idPS00850
Number of Residues9
DetailsGLY_RADICAL_1 Glycine radical domain signature. IvRIAGYSA
ChainResidueDetails
BILE798-ALA806

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000305|PubMed:30962433
ChainResidueDetails
BCYS466
DCYS466
CCYS466
ACYS466

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:30962433
ChainResidueDetails
BGLU468
DGLU468
CGLU468
AGLU468

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:30962433
ChainResidueDetails
BARG187
CGLN191
CCYS466
CARG676
AARG187
AGLN191
ACYS466
AARG676
BGLN191
BCYS466
BARG676
DARG187
DGLN191
DCYS466
DARG676
CARG187

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Glycine radical => ECO:0000255|PROSITE-ProRule:PRU00493
ChainResidueDetails
BGLY803
DGLY803
CGLY803
AGLY803

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon