1bm0

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spinqualitylabelsall models PDB ID 1bm0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1bm0, resolution 2.50Å ()
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, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

Overview

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.

About this Structure

1BM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 11:41:00 2008