Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7BZ4

The mutant variant of PNGM-1. H279 was substituted for alanine to study metal coordination.

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0042780biological_processtRNA 3'-end processing
A0042781molecular_function3'-tRNA processing endoribonuclease activity
A0046872molecular_functionmetal ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0042780biological_processtRNA 3'-end processing
B0042781molecular_function3'-tRNA processing endoribonuclease activity
B0046872molecular_functionmetal ion binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0042780biological_processtRNA 3'-end processing
C0042781molecular_function3'-tRNA processing endoribonuclease activity
C0046872molecular_functionmetal ion binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0042780biological_processtRNA 3'-end processing
D0042781molecular_function3'-tRNA processing endoribonuclease activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS91
AHIS93
AHIS188
AASP210
AHOH559
AHOH608

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BASP210
BHOH505
BHOH577
BHIS91
BHIS93
BHIS188

site_idAC3
Number of Residues7
Detailsbinding site for residue ZN C 401
ChainResidue
CHIS91
CHIS93
CHIS188
CASP210
CHOH503
CHOH522
CHOH547

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN D 401
ChainResidue
DHIS91
DHIS93
DHIS188
DASP210
DHOH568
DHOH611

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon