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› 6xj5

X-ray diffraction
3.11Å resolution

Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design

Released:
DOI: 10.2210/pdb6xj5/pdb
Model geometry
Fit model/data
PDB entry 6xj5 coloured by chain, front view.
PDB entry 6xj5 coloured by chain, side view.
PDB entry 6xj5 coloured by chain, top view.
Source organism: Pseudomonas sp. RS-16
Primary publication:
A Bis(imidazole)-based cysteine labeling tool for metalloprotein assembly.
Ahmad R, Tyryshkin AM, Xie L, Hansen WA, Yachnin BJ, Emge TJ, Mashrai A, Khare SD, Knapp S
J Inorg Biochem 244 112206 (2023)
PMID: 37030124

Function and Biology Details

Reaction catalysed: 
[Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups., Release of C-terminal glutamate residues from a wide range of N-acylatingmoieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl,folyl and pteroyl groups.]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139103 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxypeptidase G2 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 411 amino acids
Theoretical weight: 44.01 KDa
Source organism: Pseudomonas sp. RS-16
Expression system: Escherichia coli
UniProt:
  • Canonical: P06621 (Residues: 24-415; Coverage: 100%)
Gene name: cpg2
Sequence domains:
Carboxypeptidase G2 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 411 amino acids
Theoretical weight: 44.2 KDa
Source organism: Pseudomonas sp. RS-16
Expression system: Escherichia coli
UniProt:
  • Canonical: P06621 (Residues: 24-415; Coverage: 100%)
Gene name: cpg2
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 56 x ZN
Ligand SO4 2 x SO4
1 modified residue:
Ligand V44 4 x V44

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 72.12Å b: 188.46Å c: 124.5Å
α: 90° β: 90.17° γ: 90°
R-values:
R R work R free
0.273 0.271 0.309
Expression system: Escherichia coli

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