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1bm0

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1bm0, resolution 2.50Å ()

Domains:

ALBUMIN

Structural annotation:
Resources:	CATH : 1Bm0A03, 1Bm0A06, 1Bm0A05, 1Bm0A02, 1Bm0A04, 1Bm0A01, 1Bm0B01, 1Bm0B02, 1Bm0B04, 1Bm0B05, 1Bm0B06, 1Bm0B03 InterPro : Ipr000264, Ipr001703, Ipr014760 Pfam : PF00273 SCOP : d1bm0a3, d1bm0a2, d1bm0a1, d1bm0b2, d1bm0b3, d1bm0b1 UniProt : P02768

Functional annotation:
Cellular component:	extracellular region extracellular space protein complex
Biological process:	hemolysis by symbiont of host red blood cells maintenance of mitochondrion localization negative regulation of apoptosis cellular response to starvation negative regulation of non-apoptotic programmed cell death transport
Molecular function:	DNA binding antioxidant activity protein binding copper ion binding toxin binding pyridoxal phosphate binding drug binding oxygen binding metal ion binding lipid binding fatty acid binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

Publication Abstract from PubMed

A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.

Crystal structure of human serum albumin at 2.5 A resolution., Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K, Protein Eng. 1999 Jun;12(6):439-46. PMID:10388840

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1BM0 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K. Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. PMID:10388840

Page seeded by OCA on Wed Feb 18 00:08:08 2009

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1bm0

From Proteopedia

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

About this Structure

Reference

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