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Ketoreductase lbcr mutant - M6

Analyse Ketoreductase lbcr mutant - M6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZFM
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: 9 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	3-oxoacyl-acyl carrier protein reductase	protein	248	47% helix, 17% strand	Q03TH6

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	546	0.76	0.83	93	empty
2	447	0.72	0.82	49	empty
3	424	0.71	0.82	49	empty
4	505	0.69	0.79	49	empty
5	393	0.63	0.78	48	empty

Interfaces

6 interfaces between chains.

C–D · 1786 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1762 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1442 Å² buried · 17 hydrogen bonds · protein-protein
A–D · 1427 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 122 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5ZFM · Ketoreductase LbCR mutant - M6 · 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 Q03TH6
Elsewhere: RCSB PDB 5ZFM · PDBe 5ZFM · UniProt Q03TH6

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