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Bacteroides thetaiotaomicron VPI5482 BTAXE1

Analyse Bacteroides thetaiotaomicron VPI5482 BTAXE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DWC
Type: protein
Length: 1,055 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase
UniProt: Q8A909
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Xylanase	protein	264	35% helix, 22% strand	Q8A909
D	Xylanase	protein	263	36% helix, 21% strand	Q8A909

Pockets

3 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	1091	0.82	0.83	100	empty
2	1027	0.80	0.82	100	empty
3	58	0.37	0.79	13	empty

Interfaces

5 interfaces between chains.

A–C · 1136 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 294 Å² buried · 1 hydrogen bond · protein-protein
A–D · 213 Å² buried · 1 hydrogen bond · protein-protein
C–D · 109 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 109 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7DWC · Bacteroides thetaiotaomicron VPI5482 BTAxe1 · 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 Q8A909
Elsewhere: RCSB PDB 7DWC · PDBe 7DWC · UniProt Q8A909

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