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Crystallographic structure of paenibacillus xylanivorans GH11

Analyse Crystallographic structure of paenibacillus xylanivorans GH11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KV0
Type: protein
Length: 372 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase
EC: 3.2.1.8
UniProt: A0A0M9BNX9
Pockets: 4 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	186	5% helix, 63% strand	A0A0M9BNX9

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.52	0.82	19	empty
2	150	0.45	0.76	24	empty
3	65	0.32	0.76	16	EDO
4	59	0.29	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 826 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7KV0 · Crystallographic structure of Paenibacillus xylanivorans GH11 · the same entry in another collection · chain B against B, 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 A0A0M9BNX9
Elsewhere: RCSB PDB 7KV0 · PDBe 7KV0 · UniProt A0A0M9BNX9

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