MolNFT v1 · #48043 · protein

Crystal structure of 3-oxoacyl-[acyl carrier protein] reductase TTHA0415 from thermus thermophilus

2PH3: “Crystal structure of 3-oxoacyl-[acyl carrier protein] reductase TTHA0415 from thermus thermophilus”. X-ray diffraction, 4 pockets (best druggability 0.77). MolNFT v1 #48043 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 2PH3
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl carrier protein] reductase
EC: 1.1.1.100
UniProt: Q5SL78
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acyl carrier protein] reductase (EC 1.1.1.100)	protein	245	51% helix, 17% strand	Q5SL78
B	3-oxoacyl-[acyl carrier protein] reductase (EC 1.1.1.100)	protein	237	54% helix, 14% strand	Q5SL78

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	639	0.77	0.83	52	empty
2	626	0.71	0.79	61	empty
3	111	0.55	0.83	19	empty
4	56	0.36	0.79	11	empty

Interfaces

1 interface between chains.

A–B · 1708 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

2PH3 · Crystal structure of 3-oxoacyl-[acyl carrier protein] reductase TTHA0415 from Thermus… · 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 Q5SL78
Elsewhere: RCSB PDB 2PH3 · PDBe 2PH3 · UniProt Q5SL78

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