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3O90

High resolution crystal structures of Streptococcus pneumoniae nicotinamidase with trapped intermediates provide insights into catalytic mechanism and inhibition by aldehydes

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 192
ChainResidue
AASP53
AHIS55
AGLU64
AHIS71

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 192
ChainResidue
BASP53
BHIS55
BGLU64
BHIS71
BHOH560

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 192
ChainResidue
CASP53
CHIS55
CHIS71

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 192
ChainResidue
DASP53
DHIS55
DGLU64
DHIS71

Functional Information from PROSITE/UniProt
site_idPS01039
Number of Residues14
DetailsSBP_BACTERIAL_3 Bacterial extracellular solute-binding proteins, family 3 signature. GYDIEIVKpAVASI
ChainResidueDetails
AGLY148-ILE161

222415

PDB entries from 2024-07-10

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