MolNFT v1 · #17197 · protein

The trichoderma reesei CEL12A P201C mutant, structure at 1.7 a resolution

1OLQ · Endo-beta-1,4-glucanase: “The trichoderma reesei CEL12A P201C mutant, structure at 1.7 a resolution”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.78). MolNFT v1 #17197 on GenesisL1: 3D structure, binding sites…

PDB: 1OLQ
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-glucanase
EC: 3.2.1.4
UniProt: O00095
Ligands: NAG
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-beta-1,4-glucanase (EC 3.2.1.4)	protein	218	6% helix, 57% strand	O00095

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	935	0.78	0.80	104	empty

Interfaces

1 interface between chains.

A–B · 854 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 2 glycan, 2 modified (disulfide, N-glycosylation, cyclization).

Compared structures

1OLQ · The Trichoderma reesei cel12a P201C mutant, structure at 1.7 A resolution · 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 O00095
Elsewhere: RCSB PDB 1OLQ · PDBe 1OLQ · UniProt O00095

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