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5HXU

Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of Toblerone fold enzymes

Functional Information from GO Data
ChainGOidnamespacecontents
A0006212biological_processuracil catabolic process
A0016787molecular_functionhydrolase activity
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0046872molecular_functionmetal ion binding
A0047694molecular_functionbarbiturase activity
B0006212biological_processuracil catabolic process
B0016787molecular_functionhydrolase activity
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0046872molecular_functionmetal ion binding
B0047694molecular_functionbarbiturase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 401
ChainResidue
AARG247
AARG254

site_idAC2
Number of Residues14
Detailsbinding site for residue MHA A 402
ChainResidue
AASN194
ASER230
ASER231
ALYS328
ASER347
AVAL348
AHOH540
AGLY46
AGLY47
AASP50
AARG53
ASER83
AGLY84
AMET190

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 403
ChainResidue
AGLU301
AALA350
AGLN353
AGLY354
APRO355
AGLY358

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AARG34
AALA102

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 B 401
ChainResidue
BGLU110
BARG247
BARG254

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 402
ChainResidue
BASP155
BHIS157
BASN245
BARG254
BHOH573

site_idAC7
Number of Residues14
Detailsbinding site for residue MHA B 403
ChainResidue
BLYS41
BGLY46
BARG53
BTRP82
BSER83
BGLY84
BLYS162
BMET190
BASN194
BSER230
BSER231
BLYS328
BSER347
BVAL348

site_idAC8
Number of Residues6
Detailsbinding site for residue NA B 404
ChainResidue
BGLU301
BALA350
BGLN353
BGLY354
BPRO355
BGLY358

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AKLIDDGVleaD
ChainResidueDetails
AALA22-ASP33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues270
DetailsRegion: {"description":"RU B","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues116
DetailsRegion: {"description":"RU C","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28235873","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues102
DetailsRegion: {"description":"RU A","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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