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Mycobacterium tuberculosis DPRE1 - hexagonal crystal form

Analyse Mycobacterium tuberculosis DPRE1 - hexagonal crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FEH
Type: protein
Length: 419 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidoreductase DPRE1
EC: 1.-.-.-
UniProt: P72056
Ligands: FAD
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxidoreductase DPRE1 (EC 1.-.-.-)	protein	419	30% helix, 26% strand	P72056

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 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	712	0.79	0.83	74	FAD

Compared structures

4FEH · Mycobacterium tuberculosis DprE1 - hexagonal crystal form · 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 P72056
Elsewhere: RCSB PDB 4FEH · PDBe 4FEH · UniProt P72056

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