PDB entry 1b56

HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN

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The structure was published by Hohoff, C., Borchers, T., Rustow, B., Spener, F., and van Tilbeurgh, H., in 1999 in a paper entitled "Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.05 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of FATTY ACID BINDING PROTEIN. This molecule has the UniProt identifier Q01469 (FABP5_HUMAN). The sample contained 135 residues which is 100% of the natural sequence. Out of 135 residues 132 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain	Name	UniProt	Name of source organism	% of UniProt sequence present in the sample	Residues in the sample molecules	% of residues observed
A	FATTY ACID BINDING PROTEIN	Q01469 (1-135) (FABP5_HUMAN)	Homo sapiens	100%	135	98%

This entry contains 1 unique UniProt protein:

UniProt accession	Name	Organism	PDB
Q01469 (1 - 135)	FATTY ACID BINDING PROTEIN	Homo sapiens	Related PDB sequences UniProt coverage

Chain	Structural classification (SCOP)	Structural classification (CATH)	Sequence family (Pfam)
A (Q01469)	Fatty acid binding protein-like	Lipocalin	Lipocalin / cytosolic fatty-acid binding protein family

Chain ID	Molecular function (GO)	Cellular component (GO)	Biological process (GO)
A (Q01469)	Transporter activity, Binding, Fatty acid binding, Protein binding, Lipid binding	Cytoplasm	Glucose metabolic process, Lipid metabolic process, Phosphatidylcholine biosynthetic process, Transport, Epidermis development, Glucose transport

Chain	InterPro annotation
A	Cytosolic fatty-acid binding, Lipocalin/cytosolic fatty-acid binding protein domain, Calycin-like, Calycin