spacer
spacer

PDBsum entry 4is4

Go to PDB code: 
protein Protein-protein interface(s) links
Ligase PDB id
4is4
Jmol
Contents
Protein chains
339 a.a.
(+ 3 more) 306 a.a.
Waters ×969
PDB id:
4is4
Name: Ligase
Title: The glutamine synthetase from the dicotyledonous plant m. Tr is a decamer
Structure: Glutamine synthetase. Chain: a, b, c, d, e, f, g, h, i, j. Engineered: yes
Source: Medicago truncatula. Barrel medic. Organism_taxid: 3880. Gene: mtr_6g071070. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.35Å     R-factor:   0.177     R-free:   0.217
Authors: A.R.Seabra,H.Carvalho,P.J.B.Pereira
Key ref: E.Torreira et al. (2014). The structures of cytosolic and plastid-Located gluta synthetases from medicago truncatula reveal a common dynamic architecture. Acta crystallogr ,Sect d, 70, 981.
Date:
16-Jan-13     Release date:   09-Apr-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O04998  (O04998_MEDTR) -  Glutamine synthetase
Seq:
Struc:
356 a.a.
339 a.a.
Protein chains
Pfam   ArchSchema ?
O04998  (O04998_MEDTR) -  Glutamine synthetase
Seq:
Struc:
356 a.a.
306 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H, I, J: E.C.6.3.1.2  - Glutamate--ammonia ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
ATP
+ L-glutamate
+ NH(3)
= ADP
+ phosphate
+ L-glutamine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     nitrogen compound metabolic process   2 terms 
  Biochemical function     catalytic activity     5 terms