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6VXE

Crystal structure of hydroxyproline dehydratase (HypD) from Clostridioides difficile with substrate trans-4-hydroxy-L-proline bound

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 Residues12
Detailsbinding site for residue HYP A 801
ChainResidue
APHE152
ATYR450
ATHR645
AHOH1009
AHIS160
ATRP277
AASP278
ASER334
APHE340
ACYS434
AGLU436
ALEU447

site_idAC2
Number of Residues11
Detailsbinding site for residue HYP B 801
ChainResidue
BHIS160
BTRP277
BASP278
BSER334
BPHE340
BGLY433
BCYS434
BGLU436
BLEU447
BTYR450
BTHR645

site_idAC3
Number of Residues12
Detailsbinding site for residue HYP C 801
ChainResidue
CPHE152
CHIS160
CTRP277
CASP278
CSER334
CPHE340
CGLY433
CCYS434
CGLU436
CLEU447
CTYR450
CTHR645

site_idAC4
Number of Residues10
Detailsbinding site for residue HYP D 801
ChainResidue
DPHE152
DTRP277
DASP278
DSER334
DPHE340
DCYS434
DGLU436
DLEU447
DTYR450
DTHR645

site_idAC5
Number of Residues11
Detailsbinding site for residue HYP E 801
ChainResidue
EPHE152
ETRP277
EASP278
EGLU333
ESER334
EPHE340
ECYS434
EGLU436
ELEU447
ETYR450
ETHR645

site_idAC6
Number of Residues11
Detailsbinding site for residue HYP F 801
ChainResidue
FPHE152
FHIS160
FTRP277
FASP278
FSER334
FPHE340
FCYS434
FGLU436
FLEU447
FTYR450
FTHR645

site_idAC7
Number of Residues11
Detailsbinding site for residue HYP G 801
ChainResidue
GPHE152
GHIS160
GTRP277
GASP278
GGLU333
GSER334
GPHE340
GCYS434
GGLU436
GTYR450
GTHR645

site_idAC8
Number of Residues11
Detailsbinding site for residue HYP H 801
ChainResidue
HHIS160
HTRP277
HASP278
HGLU333
HSER334
HPHE340
HCYS434
HGLU436
HLEU447
HTYR450
HTHR645

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5248
DetailsDomain: {"description":"PFL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00887","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues952
DetailsDomain: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28183913","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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