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Cellotetraose complex of cellulase 12A from thermotoga maritima

Analyse Cellotetraose complex of cellulase 12A from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AMM
Type: protein
Length: 516 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-glucanase
EC: 3.2.1.4
UniProt: Q60032
Ligands: BGC
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-glucanase (EC 3.2.1.4)	protein	255	9% helix, 57% strand	Q60032
B	Endo-1,4-beta-glucanase (EC 3.2.1.4)	protein	261	9% helix, 57% strand	Q60032

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 8 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	188	0.62	0.83	27	BGC
2	189	0.61	0.82	26	BGC
3	57	0.48	0.85	15	empty
4	65	0.36	0.78	16	empty
5	55	0.31	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 561 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3AMM · Cellotetraose complex of cellulase 12A from thermotoga maritima · 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 Q60032
Elsewhere: RCSB PDB 3AMM · PDBe 3AMM · UniProt Q60032

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