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Crystal structure of C205F mutant of PKS18 from mycobacterium tuberculosis

Analyse Crystal structure of C205F mutant of PKS18 from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TEE
Type: protein
Length: 1,454 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PKS18
EC: 2.3.1.74
UniProt: Q7D8I1
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	PKS18 (EC 2.3.1.74)	protein	368	40% helix, 26% strand	Q7D8I1
B, D	PKS18 (EC 2.3.1.74)	protein	359	43% helix, 26% strand	Q7D8I1

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	1102	0.81	0.82	109	empty
2	64	0.73	0.98	26	empty
3	66	0.73	0.98	24	empty
4	63	0.73	0.97	24	empty
5	60	0.73	0.99	25	empty

Interfaces

4 interfaces between chains.

C–D · 2417 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 2411 Å² buried · 22 hydrogen bonds · protein-protein
A–C · 924 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 101 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1TEE · Crystal structure of C205F mutant of PKS18 from Mycobacterium tuberculosis · 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 Q7D8I1
Elsewhere: RCSB PDB 1TEE · PDBe 1TEE · UniProt Q7D8I1

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