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6S7Q

Crystal structure of ergothioneine degrading enzyme Ergothionase from Treponema denticola in complex with desmethyl-ergothioneine sulfonic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004397molecular_functionhistidine ammonia-lyase activity
A0006548biological_processL-histidine catabolic process
A0016841molecular_functionammonia-lyase activity
B0003824molecular_functioncatalytic activity
B0004397molecular_functionhistidine ammonia-lyase activity
B0006548biological_processL-histidine catabolic process
B0016841molecular_functionammonia-lyase activity
C0003824molecular_functioncatalytic activity
C0004397molecular_functionhistidine ammonia-lyase activity
C0006548biological_processL-histidine catabolic process
C0016841molecular_functionammonia-lyase activity
D0003824molecular_functioncatalytic activity
D0004397molecular_functionhistidine ammonia-lyase activity
D0006548biological_processL-histidine catabolic process
D0016841molecular_functionammonia-lyase activity
E0003824molecular_functioncatalytic activity
E0004397molecular_functionhistidine ammonia-lyase activity
E0006548biological_processL-histidine catabolic process
E0016841molecular_functionammonia-lyase activity
F0003824molecular_functioncatalytic activity
F0004397molecular_functionhistidine ammonia-lyase activity
F0006548biological_processL-histidine catabolic process
F0016841molecular_functionammonia-lyase activity
G0003824molecular_functioncatalytic activity
G0004397molecular_functionhistidine ammonia-lyase activity
G0006548biological_processL-histidine catabolic process
G0016841molecular_functionammonia-lyase activity
H0003824molecular_functioncatalytic activity
H0004397molecular_functionhistidine ammonia-lyase activity
H0006548biological_processL-histidine catabolic process
H0016841molecular_functionammonia-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue KZ5 A 501
ChainResidue
ATYR54
AALA408
AGLU412
BARG281
DGLY380
DTHR381
DLYS384
AVAL60
AGLY61
AHIS84
AGLU143
AILE146
ASER195
AASN311
APHE327

site_idAC2
Number of Residues14
Detailsbinding site for residue KZ5 C 502
ChainResidue
BGLY380
BTHR381
BLYS384
CTYR54
CVAL60
CGLY61
CHIS84
CGLU143
CILE146
CSER195
CASN311
CALA408
CGLU412
DARG281

site_idAC3
Number of Residues16
Detailsbinding site for residue KZ5 D 501
ChainResidue
AGLY380
ATHR381
ALYS384
CARG281
DTYR54
DVAL60
DGLY61
DHIS84
DGLU143
DILE146
DSER195
DASN311
DPHE327
DALA408
DGLU412
DHOH606

site_idAC4
Number of Residues13
Detailsbinding site for residue KZ5 F 501
ChainResidue
EARG281
FTYR54
FVAL60
FGLY61
FHIS84
FGLU143
FSER195
FASN311
FALA408
FGLU412
GGLY380
GTHR381
GLYS384

site_idAC5
Number of Residues14
Detailsbinding site for residue KZ5 G 501
ChainResidue
FGLY380
FTHR381
FLYS384
GTYR54
GVAL60
GGLY61
GHIS84
GGLU143
GILE146
GSER195
GASN311
GPHE327
GGLU412
HARG281

site_idAC6
Number of Residues21
Detailsbinding site for Di-peptide KZ5 C 501 and LYS C 384
ChainResidue
AARG281
BTYR54
BVAL60
BGLY61
BHIS84
BSER139
BILE141
BGLU143
BILE146
BSER195
BASN311
BPHE327
BALA408
BGLU412
CGLY380
CTHR381
CILE382
CGLN383
CTHR385
CPHE386
CMET388

site_idAC7
Number of Residues19
Detailsbinding site for Di-peptide KZ5 E 501 and LYS E 384
ChainResidue
ETHR387
EMET388
HTYR54
HVAL60
HGLY61
HHIS84
HSER139
HILE146
HTHR147
HSER195
HASN311
HLEU407
HGLU412
EGLY380
ETHR381
EILE382
EGLN383
ETHR385
EPHE386

site_idAC8
Number of Residues17
Detailsbinding site for Di-peptide KZ5 H 501 and LYS H 384
ChainResidue
ETYR54
EGLY61
EHIS84
ESER139
EILE141
EGLU143
EILE146
EALA408
EGLU412
FARG281
HGLY380
HTHR381
HILE382
HGLN383
HTHR385
HPHE386
HMET388

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PDB entries from 2024-09-04

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