Research workbench

E.COLI kas I H298E mutation

Analyse E.COLI kas I H298E mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BYY
Type: protein
Length: 1,620 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl-carrier-protein] synthase I
EC: 2.3.1.41
UniProt: P14926
Ligands: NH4
Pockets: 11 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	3-oxoacyl-[acyl-carrier-protein] synthase I (EC 2.3.1.41)	protein	405	38% helix, 22% strand	P14926

Ligands and binding sites

NH4 · Ammonium ion · ion · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

11 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	200	0.74	0.89	48	empty
2	53	0.71	0.98	17	empty
3	162	0.65	0.86	36	empty
4	149	0.65	0.86	33	empty
5	156	0.63	0.85	30	empty

Interfaces

3 interfaces between chains.

A–B · 3003 Å² buried · 49 hydrogen bonds · protein-protein
C–D · 2988 Å² buried · 55 hydrogen bonds · protein-protein
A–C · 427 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2BYY · E.coli KAS I H298E Mutation · 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 P14926
Elsewhere: RCSB PDB 2BYY · PDBe 2BYY · UniProt P14926

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