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Maeb pta domain R535E mutant

Analyse Maeb pta domain R535E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZNE
Type: protein
Length: 2,029 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malate dehydrogenase
EC: 1.1.1.40
UniProt: Q6MM15
Pockets: 20 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, F, E	Malate dehydrogenase (EC 1.1.1.40)	protein	338	49% helix, 17% strand	Q6MM15
C	Malate dehydrogenase (EC 1.1.1.40)	protein	339	50% helix, 17% strand	Q6MM15

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.74	0.87	24	empty
2	877	0.73	0.77	82	empty
3	816	0.71	0.77	73	empty
4	288	0.70	0.84	26	empty
5	310	0.70	0.83	27	empty

Interfaces

12 interfaces between chains.

A–B · 1726 Å² buried · 15 hydrogen bonds · protein-protein
D–C · 1698 Å² buried · 15 hydrogen bonds · protein-protein
F–E · 1689 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 316 Å² buried · 2 hydrogen bonds · protein-protein
E–C · 313 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6ZNE · MaeB PTA domain R535E mutant · 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 Q6MM15
Elsewhere: RCSB PDB 6ZNE · PDBe 6ZNE · UniProt Q6MM15

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