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Structural and active site modification studies implicate glu, TRP and arg in the activity of xylanase from alkalophilic bacillus sp. (ncl 87-6-10).

Analyse Structural and active site modification studies implicate glu, TRP and arg in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F6B
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Family 11 xylanase
EC: 3.2.1.8
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 64% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Family 11 xylanase (EC 3.2.1.8)	protein	206	7% helix, 64% strand	—

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	755	0.69	0.76	67	empty

Interfaces

1 interface between chains.

A–B · 546 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2F6B · Structural and active site modification studies implicate Glu, Trp and Arg in the… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2F6B · PDBe 2F6B

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