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Mycobacterium smegmatis DPRE1 - monoclinic crystal form

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

PDB: 4G3U
Type: protein
Length: 692 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidoreductase DPRE1
EC: 1.-.-.-
UniProt: A0R607
Pockets: 6 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Oxidoreductase DPRE1 (EC 1.-.-.-)	protein	346	30% helix, 25% strand	A0R607

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	321	0.62	0.79	39	empty
2	149	0.61	0.84	22	empty
3	356	0.58	0.76	40	empty
4	336	0.56	0.75	46	empty
5	240	0.55	0.78	30	empty

Interfaces

1 interface between chains.

A–B · 311 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4G3U · Mycobacterium smegmatis DprE1 - monoclinic crystal form · the same entry in another collection · chain A against A, TM-score 1.00
A0R607 · AlphaFold monomer V2.0 prediction for decaprenylphosphoryl-beta-D- ribose oxidase (A0R607) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 A0R607
Elsewhere: RCSB PDB 4G3U · PDBe 4G3U · UniProt A0R607

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