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

5HY1

high resolution structure of barbiturase

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue WDL A 401
ChainResidue
AGLY46
ASER347
AVAL348
AHOH502
AARG53
ASER83
AGLY84
AMET190
AASN194
ASER230
ASER231
ALYS328

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 402
ChainResidue
AGLU301
AALA350
AGLN353
AGLY354
APRO355
AGLY358

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 403
ChainResidue
AARG34
AALA102

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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
ALYS162

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
ASER230

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:28235873
ChainResidueDetails
AARG53
AGLY354
APRO355
AGLY358
ASER83
AASN194
ASER230
AGLU301
ALYS328
ASER347
AALA350
AGLN353

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
AHIS324

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon