MolNFT v1 · #502549 · protein

AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q9HFH0)

Q9HFH0: “AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q9HFH0)”. 1 pocket (best druggability 0.58). MolNFT v1 #502549 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q9HFH0
Type: protein
Length: 223 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x989A13EeC035A3Ebf3E3E2eA5EaE1293777938cF
Molecule: Endo-1,4-beta-xylanase C
UniProt: Q9HFH0
Pockets: 1 · best druggability 0.58

Structure

1 distinct chain · 6% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase C	protein	223	6% helix, 58% strand	Q9HFH0

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	244	0.58	0.79	31	empty

Compared structures

3WP3 · Xylanase 11C from Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) · an experimental structure of the same protein · chain A against A, TM-score 0.84
3WP3 · Xylanase 11C from talaromyces cellulolyticus (formerly known as acremonium cellulolyticus) · an experimental structure of the same protein · chain A against A, TM-score 0.84
1TE1 · Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I) · an experimental structure of the same protein · chain A against B, TM-score 0.84
1TE1 · Crystal structure of family 11 xylanase in complex with inhibitor (xip-I) · an experimental structure of the same protein · chain A against B, TM-score 0.84

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 Q9HFH0
Elsewhere: UniProt Q9HFH0 · AlphaFold DB Q9HFH0

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