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Crystal structure of antigen 85C co-crystallized with ebselen

Analyse Crystal structure of antigen 85C co-crystallized with ebselen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QDU
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diacylglycerol ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C
EC: 2.3.1.122, 2.3.1.20
UniProt: P9WQN9
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diacylglycerol ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C (EC 2.3.1.122, 2.3.1.20)	protein	283	37% helix, 17% strand	P9WQN9

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.30	0.75	15	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

4QDU · Crystal structure of Antigen 85C co-crystallized with ebselen · the same entry in another collection · chain A against A, TM-score 1.00
P9WQN9 · AlphaFold monomer V2.0 prediction for diacylglycerol ACYLTRANSFERASE/MYCOLYLTRANSFERASE… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P9WQN9
Elsewhere: RCSB PDB 4QDU · PDBe 4QDU · UniProt P9WQN9

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