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Ketoreductase lbcr mutant - M8

Analyse Ketoreductase lbcr mutant - M8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZI0
Type: protein
Length: 992 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-acyl carrier protein reductase
UniProt: Q03TH6
Pockets: 8 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	3-oxoacyl-acyl carrier protein reductase	protein	248	46% helix, 17% strand	Q03TH6

Pockets

8 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	870	0.81	0.84	79	empty
2	453	0.66	0.78	52	empty
3	385	0.61	0.77	51	empty
4	152	0.59	0.83	27	empty
5	143	0.57	0.83	26	empty

Interfaces

6 interfaces between chains.

A–B · 1763 Å² buried · 19 hydrogen bonds · protein-protein
C–D · 1730 Å² buried · 16 hydrogen bonds · protein-protein
A–D · 1446 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1444 Å² buried · 16 hydrogen bonds · protein-protein
A–C · 112 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5ZI0 · Ketoreductase LbCR mutant - M8 · the same entry in another collection · chain B against B, 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 Q03TH6
Elsewhere: RCSB PDB 5ZI0 · PDBe 5ZI0 · UniProt Q03TH6

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