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1YNY

Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
B0004157molecular_functiondihydropyrimidinase activity
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 471
ChainResidue
AHIS58
AHIS60
ALYS150
AASP315
AMN472
AHOH1128

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 472
ChainResidue
AMN471
AHOH1112
AHOH1128
ALYS150
AHIS183
AHIS239

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 471
ChainResidue
BHIS58
BHIS60
BLYS150
BASP315
BMN472
BHOH5110

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 472
ChainResidue
BLYS150
BHIS183
BHIS239
BMN471
BHOH5109
BHOH5110

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
AASP315

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
BASP315

219140

PDB entries from 2024-05-01

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