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E269A mutant of highly active efbsh

Analyse E269A mutant of highly active efbsh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A8T
Type: protein
Length: 1,292 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile salt hydrolase
UniProt: C7CXJ5
Pockets: 18 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Bile salt hydrolase	protein	323	20% helix, 32% strand	C7CXJ5

Pockets

18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	931	0.87	0.88	92	empty
2	322	0.76	0.88	50	empty
3	303	0.76	0.88	45	empty
4	236	0.75	0.89	30	empty
5	340	0.71	0.84	47	empty

Interfaces

6 interfaces between chains.

C–D · 3259 Å² buried · 63 hydrogen bonds · protein-protein
A–B · 3175 Å² buried · 61 hydrogen bonds · protein-protein
A–D · 1482 Å² buried · 26 hydrogen bonds · protein-protein
B–C · 1478 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 315 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6A8T · E269A mutant of highly active EfBSH · 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 C7CXJ5
Elsewhere: RCSB PDB 6A8T · PDBe 6A8T · UniProt C7CXJ5

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