› 1g5w

Solution NMR

SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN

Released:
DOI: 10.2210/pdb1g5w/pdb
PDB entry 1g5w coloured by chain, ensemble of 20 models, front view.
PDB entry 1g5w coloured by chain, ensemble of 20 models, side view.
PDB entry 1g5w coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP).
Lücke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Rüterjans H
Biochem J 354 259-66 (2001)
PMID: 11171102

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid-binding protein, heart Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05413 (Residues: 2-133; Coverage: 99%)
Gene names: FABP11, FABP3, MDGI
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing and energy-minimization
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Insights into binding of fatty acids by fatty acid binding proteins.
Hanhoff et al. (2002)
1 more

5 mentions without citation

Relation between native ensembles and experimental structures of proteins.
Best et al. (2006)
4 more