4GDX
Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex
- PDB DOI: https://doi.org/10.2210/pdb4GDX/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Pichia
- Mutation(s): No 
- Deposited: 2012-08-01 Released: 2013-09-25 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.67 Å
- R-Value Free: 0.174 
- R-Value Work: 0.145 
- R-Value Observed: 0.147 
This is version 1.4 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Gamma-glutamyltranspeptidase 1 heavy chain | 374 | Homo sapiens | Mutation(s): 0  Gene Names: GGT, GGT1 EC: 2.3.2.2 (PDB Primary Data), 3.4.19.13 (PDB Primary Data), 3.4.19.14 (PDB Primary Data) | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P19440 (Homo sapiens) Explore P19440  Go to UniProtKB:  P19440 | |||||
PHAROS:  P19440 GTEx:  ENSG00000100031  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P19440 | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Gamma-glutamyltranspeptidase 1 light chain | 195 | Homo sapiens | Mutation(s): 0  Gene Names: GGT, GGT1 EC: 2.3.2.2 (PDB Primary Data), 3.4.19.13 (PDB Primary Data), 3.4.19.14 (PDB Primary Data) | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P19440 (Homo sapiens) Explore P19440  Go to UniProtKB:  P19440 | |||||
PHAROS:  P19440 GTEx:  ENSG00000100031  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P19440 | ||||
Sequence AnnotationsExpand | |||||
|
Small Molecules
Ligands 4 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | C [auth A] D [auth A] E [auth A] F [auth A] G [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
GLU Query on GLU | K [auth B] | GLUTAMIC ACID C5 H9 N O4 WHUUTDBJXJRKMK-VKHMYHEASA-N | |||
CL Query on CL | H [auth A], L [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M | |||
NA Query on NA | I [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.67 Å
- R-Value Free: 0.174 
- R-Value Work: 0.145 
- R-Value Observed: 0.147 
- Space Group: C 2 2 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 105.524 | α = 90 |
b = 125.247 | β = 90 |
c = 104.468 | γ = 90 |
Software Name | Purpose |
---|---|
HKL-2000 | data collection |
MOLREP | phasing |
PHENIX | refinement |
HKL-2000 | data reduction |
SCALA | data scaling |
Entry History 
Deposition Data
- Released Date: 2013-09-25  Deposition Author(s): West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.
Revision History (Full details and data files)
- Version 1.0: 2013-09-25
Type: Initial release - Version 1.1: 2013-10-16
Changes: Database references - Version 1.2: 2013-11-27
Changes: Database references - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Database references, Derived calculations, Structure summary - Version 1.4: 2023-09-13
Changes: Data collection, Database references, Refinement description, Structure summary