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Crystal structure of thrombin mutant E14EA/D14LA/E18A/S195A

Analyse Crystal structure of thrombin mutant E14EA/D14LA/E18A/S195A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H6S
Type: protein
Length: 282 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prothrombin
EC: 3.4.21.5
UniProt: P00734
Ligands: NA
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prothrombin (EC 3.4.21.5)	protein	31	32% helix, 0% strand	P00734
B	Prothrombin (EC 3.4.21.5)	protein	251	13% helix, 34% strand	P00734

Ligands and binding sites

NA · Sodium ion · metal · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	212	0.52	0.77	29	empty

Interfaces

1 interface between chains.

A–B · 1132 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4H6S · Crystal structure of thrombin mutant E14eA/D14lA/E18A/S195A · the same entry in another collection · chain A against A, TM-score 1.00

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 P00734
Elsewhere: RCSB PDB 4H6S · PDBe 4H6S · UniProt P00734

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