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Crystal structure of cleaved bovine antithrombin III at 3.2 ångströms resolution

Analyse Crystal structure of cleaved bovine antithrombin III at 3.2 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ATT
Type: protein
Length: 830 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antithrombin III
UniProt: P41361
Pockets: 9 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antithrombin III	protein	420	27% helix, 32% strand	P41361
B	Antithrombin III	protein	410	29% helix, 30% strand	P41361

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	158	0.61	0.84	28	empty
2	127	0.51	0.81	19	empty
3	100	0.47	0.80	27	empty
4	63	0.44	0.83	16	empty
5	78	0.38	0.77	18	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

1ATT · Crystal structure of cleaved bovine antithrombin III at 3.2 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P41361 · AlphaFold monomer V2.0 prediction for antithrombin-III (P41361) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 P41361
Elsewhere: RCSB PDB 1ATT · PDBe 1ATT · UniProt P41361

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