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Wild type TRCEL7A catalytic domain in a closed state

Analyse Wild type TRCEL7A catalytic domain in a closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TC9
Type: protein
Length: 432 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucanase
EC: 3.2.1.-
UniProt: G0RVK1
Ligands: NAG, GD3, NO3
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucanase (EC 3.2.1.-)	protein	432	13% helix, 37% strand	G0RVK1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
GD3 · Gadolinium ion · metal · chains A
NO3 · Nitrate ion · ion · chains A

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	777	0.83	0.86	83	empty

Modifications

Observed in the structure: 10 disulfide, 3 glycan, 1 modified (disulfide, N-glycosylation, cyclization).

Compared structures

5TC9 · Wild type TrCel7A catalytic domain in a closed state · 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 G0RVK1
Elsewhere: RCSB PDB 5TC9 · PDBe 5TC9 · UniProt G0RVK1

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