MolNFT v1 · #24109 · protein

Structure of endo-1,4-beta-xylanase C

1UKR · Endo-1,4-B-xylanase I: “Structure of endo-1,4-beta-xylanase C”. X-ray diffraction, 7 pockets (best druggability 0.58). MolNFT v1 #24109 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1UKR
Type: protein
Length: 724 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-B-xylanase I
EC: 3.2.1.8
UniProt: P55329
Pockets: 7 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 60% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Endo-1,4-B-xylanase I (EC 3.2.1.8)	protein	181	8% helix, 60% strand	P55329

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	258	0.58	0.79	39	empty
2	184	0.54	0.79	33	empty
3	173	0.53	0.79	28	empty
4	165	0.46	0.75	25	empty
5	85	0.41	0.78	16	empty

Interfaces

3 interfaces between chains.

B–C · 505 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 485 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 476 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1UKR · Structure of endo-1,4-beta-xylanase C · the same entry in another collection · chain A against A, TM-score 1.00
P55329 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P55329) · a predicted model of the same protein · 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 P55329
Elsewhere: RCSB PDB 1UKR · PDBe 1UKR · UniProt P55329

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