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Structure of mycobacterium tuberculosis RV1207

Analyse Structure of mycobacterium tuberculosis RV1207 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VP8
Type: protein
Length: 469 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydropteroate synthase 2
EC: 2.1.5.15
UniProt: P64139
Pockets: 6 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydropteroate synthase 2 (EC 2.1.5.15)	protein	233	48% helix, 18% strand	P64139
B	Dihydropteroate synthase 2 (EC 2.1.5.15)	protein	236	49% helix, 18% strand	P64139

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.58	0.82	22	empty
2	124	0.40	0.75	24	empty
3	68	0.37	0.78	14	empty
4	66	0.33	0.76	14	empty
5	57	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1308 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2VP8 · Structure of Mycobacterium tuberculosis Rv1207 · 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 P64139
Elsewhere: RCSB PDB 2VP8 · PDBe 2VP8 · UniProt P64139

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