Structure of PDB 4zcg Chain B Binding Site BS01

Receptor Information

>4zcg Chain B (length=189) Species: 9606 (Homo sapiens)

TAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSIT
NEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETR
HHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY

Ligand information

• Ligand ID: GLU
• InChI: InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1
• InChIKey: WHUUTDBJXJRKMK-VKHMYHEASA-N
• SMILES:
  ACDLabs 12.01: O=C(O)C(N)CCC(=O)O
  OpenEye OEToolkits 1.7.0: C(CC(=O)O)C(C(=O)O)N
  OpenEye OEToolkits 1.7.0: C(CC(=O)O)[C@@H](C(=O)O)N
  CACTVS 3.370: N[C@@H](CCC(O)=O)C(O)=O
  CACTVS 3.370: N[CH](CCC(O)=O)C(O)=O
• Formula: C5 H9 N O4
• Name: GLUTAMIC ACID
• ChEMBL: CHEMBL575060
• DrugBank: DB00142
• ZINC: ZINC000001482113
• PDB chain: 4zcg Chain B Residue 1102

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4zcg Human gamma-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
• Resolution: 2.22 Å
• Binding residue (original residue number in PDB): T381 N401 D423 S451 S452 G474
• Binding residue (residue number reindexed from 1): T1 N21 D43 S71 S72 G94
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 2.3.2.2: gamma-glutamyltransferase.
  3.4.19.13: glutathione gamma-glutamate hydrolase.
  3.4.19.14: leukotriene-C4 hydrolase.

Gene Ontology

Molecular Function

• GO:0036374 glutathione hydrolase activity

Biological Process

• GO:0006751 glutathione catabolic process

External links

• PDB: RCSB:4zcg, PDBe:4zcg, PDBj:4zcg
• PDBsum: 4zcg
• PubMed: 26013825
• UniProt: P19440|GGT1_HUMAN Glutathione hydrolase 1 proenzyme (Gene Name=GGT1)