Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 3t5c
Go to PDB code:
Ligase
PDB id
3t5c
Loading ...
Contents
Protein chains
392 a.a.
Waters
×491
PDB id:
3t5c
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Ligase
Title:
Crystal structure of n-terminal domain of facl13 from mycobacterium tuberculosis in different space group c2
Structure:
Probable chain-fatty-acid-coa ligase fadd13. Chain: a, b. Fragment: n-terminal domain (unp residues 1-396). Synonym: substrate--coa ligase, fatty-acyl-coa synthetase. Engineered: yes
Source:
Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: fadd13, mt3174, rv3089. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.09Å
R-factor:
0.208
R-free:
0.263
Authors:
A.Goyal,R.Sankaranarayanan
Key ref:
A.Goyal et al. (2012). Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis.
J Mol Biol
,
416
, 221-238.
PubMed id:
22206988
Date:
27-Jul-11
Release date:
25-Jan-12
PROCHECK
Headers
References
Protein chains
O53306
(O53306_MYCTU) -
Key:
Secondary structure
Enzyme reactions
Enzyme class:
E.C.6.2.1.-
- ?????
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
J Mol Biol
416
:221-238 (2012)
PubMed id:
22206988
Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis.
A.Goyal,
P.Verma,
M.Anandhakrishnan,
R.S.Gokhale,
R.Sankaranarayanan.
ABSTRACT
No abstract given.
'); } }