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Crystal structure of an endoglucanase pmo-5

Analyse Crystal structure of an endoglucanase pmo-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X6A
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase, putative
EC: 3.2.1.-
UniProt: Q4WP32
Ligands: MG
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endoglucanase, putative (EC 3.2.1.-)	protein	229	10% helix, 34% strand	Q4WP32

Ligands and binding sites

MG · Magnesium ion · metal · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.59	0.75	39	empty
2	65	0.52	0.86	27	empty
3	58	0.34	0.77	16	empty
4	50	0.32	0.78	15	empty

Interfaces

1 interface between chains.

A–B · 98 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5X6A · Crystal structure of an endoglucanase PMO-5 · the same entry in another collection · 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 Q4WP32
Elsewhere: RCSB PDB 5X6A · PDBe 5X6A · UniProt Q4WP32

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