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6VXC

Crystal structure of hydroxyproline dehydratase (HypD) from Clostridioides difficile

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0016829molecular_functionlyase activity
A0016835molecular_functioncarbon-oxygen lyase activity
A0019492biological_processproline salvage
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0016829molecular_functionlyase activity
B0016835molecular_functioncarbon-oxygen lyase activity
B0019492biological_processproline salvage
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0016829molecular_functionlyase activity
C0016835molecular_functioncarbon-oxygen lyase activity
C0019492biological_processproline salvage
D0003824molecular_functioncatalytic activity
D0005829cellular_componentcytosol
D0016829molecular_functionlyase activity
D0016835molecular_functioncarbon-oxygen lyase activity
D0019492biological_processproline salvage
E0003824molecular_functioncatalytic activity
E0005829cellular_componentcytosol
E0016829molecular_functionlyase activity
E0016835molecular_functioncarbon-oxygen lyase activity
E0019492biological_processproline salvage
F0003824molecular_functioncatalytic activity
F0005829cellular_componentcytosol
F0016829molecular_functionlyase activity
F0016835molecular_functioncarbon-oxygen lyase activity
F0019492biological_processproline salvage
G0003824molecular_functioncatalytic activity
G0005829cellular_componentcytosol
G0016829molecular_functionlyase activity
G0016835molecular_functioncarbon-oxygen lyase activity
G0019492biological_processproline salvage
H0003824molecular_functioncatalytic activity
H0005829cellular_componentcytosol
H0016829molecular_functionlyase activity
H0016835molecular_functioncarbon-oxygen lyase activity
H0019492biological_processproline salvage
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue GOL A 801
ChainResidue
ATRP277
AHOH913
AASP278
ASER334
APHE340
AGLY433
ACYS434
AGLU436
ATYR450
ATHR645

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL B 801
ChainResidue
BPHE152
BTRP277
BASP278
BSER334
BGLY433
BCYS434
BGLU436
BTHR645
BHOH907

site_idAC3
Number of Residues11
Detailsbinding site for residue GOL C 801
ChainResidue
CPHE152
CTRP277
CASP278
CSER334
CPHE340
CGLY433
CCYS434
CGLU436
CTYR450
CTHR645
CHOH1067

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL D 801
ChainResidue
DPHE152
DTRP277
DASP278
DSER334
DPHE340
DGLY433
DCYS434
DGLU436
DTHR645
DHOH908

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL E 801
ChainResidue
EPHE152
ETRP277
EASP278
ESER334
EPHE340
ECYS434
EGLU436
EHOH917

site_idAC6
Number of Residues10
Detailsbinding site for residue GOL F 801
ChainResidue
FPHE152
FTRP277
FASP278
FSER334
FPHE340
FGLY433
FCYS434
FGLU436
FTHR645
FHOH954

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL G 801
ChainResidue
GPHE152
GTRP277
GASP278
GSER334
GPHE340
GGLY433
GCYS434
GGLU436
GTHR645
GHOH980

site_idAC8
Number of Residues10
Detailsbinding site for residue GOL H 801
ChainResidue
HPHE152
HTRP277
HASP278
HSER334
HPHE340
HGLY433
HCYS434
HGLU436
HTHR645
HHOH961

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI3
Number of Residues8
DetailsActive site: {"description":"Cysteine radical intermediate","evidences":[{"source":"UniProtKB","id":"Q30W70","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q30W70","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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