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A trimodular GH5_4 subfamily endoglucanase structure with large unit cell

Analyse A trimodular GH5_4 subfamily endoglucanase structure with large unit cell in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XRC
Type: protein
Length: 1,593 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase
EC: 3.2.1.4
UniProt: D4P8C6
Pockets: 12 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulase (EC 3.2.1.4)	protein	531	34% helix, 28% strand	D4P8C6
B	Cellulase (EC 3.2.1.4)	protein	530	34% helix, 27% strand	D4P8C6
C	Cellulase (EC 3.2.1.4)	protein	532	34% helix, 28% strand	D4P8C6

Pockets

12 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	811	0.70	0.76	77	empty
2	791	0.69	0.76	69	empty
3	224	0.51	0.76	33	empty
4	225	0.50	0.75	31	empty
5	173	0.49	0.77	28	empty

Interfaces

1 interface between chains.

A–B · 1440 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5XRC · A Trimodular GH5_4 Subfamily Endoglucanase Structure with Large Unit Cell · 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 D4P8C6
Elsewhere: RCSB PDB 5XRC · PDBe 5XRC · UniProt D4P8C6

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