Research workbench

R207A mutant of highly active efbsh

Analyse R207A 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: 6A8Q
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: 19 · best druggability 0.85

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

19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	869	0.85	0.87	80	empty
2	327	0.73	0.85	44	empty
3	310	0.73	0.86	44	empty
4	371	0.71	0.83	55	empty
5	324	0.69	0.83	46	empty

Interfaces

6 interfaces between chains.

C–D · 3086 Å² buried · 54 hydrogen bonds · protein-protein
A–B · 3017 Å² buried · 55 hydrogen bonds · protein-protein
A–D · 1490 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1461 Å² buried · 27 hydrogen bonds · protein-protein
B–D · 319 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6A8Q · R207A 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 6A8Q · PDBe 6A8Q · UniProt C7CXJ5

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