MolNFT v1 · #179412 · protein

Crystal structure of kemp eliminase HG3

7K4P · Endo-1,4-beta-xylanase: “Crystal structure of kemp eliminase HG3”. X-ray diffraction, 4 pockets (best druggability 0.57). MolNFT v1 #179412 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7K4P
Type: protein
Length: 593 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: P23360
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	299	44% helix, 20% strand	P23360
B	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	294	44% helix, 20% strand	P23360

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	55	0.57	0.90	20	empty
2	94	0.42	0.78	19	empty
3	138	0.41	0.75	21	empty
4	87	0.37	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 362 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7K4P · Crystal structure of Kemp Eliminase HG3 · the same entry in another collection · chain A against A, TM-score 1.00
P23360 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P23360) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P23360
Elsewhere: RCSB PDB 7K4P · PDBe 7K4P · UniProt P23360

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.