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X-ray study of recombinant human serum albumin. phases determined by molecular replacement method, using low resolution structure model of tetragonal form of human serum albumin

Analyse X-ray study of recombinant human serum albumin. phases determined by molecular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UOR
Type: protein
Length: 580 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serum albumin
UniProt: P02768
Pockets: 12 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serum albumin	protein	580	47% helix, 0% strand	P02768

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1092	0.82	0.83	117	empty
2	83	0.55	0.86	18	empty
3	55	0.54	0.88	16	empty
4	80	0.47	0.82	17	empty
5	81	0.46	0.81	16	empty

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

1UOR · X-ray study of recombinant human serum albumin. phases determined by molecular… · the same entry in another collection · chain A against A, TM-score 1.00
P02768 · AlphaFold monomer V2.0 prediction for albumin (P02768) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P02768
Elsewhere: RCSB PDB 1UOR · PDBe 1UOR · UniProt P02768

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