MolNFT v1 · #76991 · protein

Crystal structure of a key regulator of virulence in mycobacterium tuberculosis

3R1F · Esx-1 secretion-associated regulator espr: “Crystal structure of a key regulator of virulence in mycobacterium tuberculosis”. X-ray diffraction, 20 pockets (best druggability 0.77). MolNFT v1 #76991 on GenesisL1: 3D structure…

PDB: 3R1F
Type: protein
Length: 2,191 residues
Chains: 18
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esx-1 secretion-associated regulator espr
UniProt: P96228
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 11 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esx-1 secretion-associated regulator espr	protein	123	67% helix, 0% strand	P96228
B, D, F, H, J, N	Esx-1 secretion-associated regulator espr	protein	130	65% helix, 0% strand	P96228
C, G	Esx-1 secretion-associated regulator espr	protein	123	68% helix, 0% strand	P96228
E	Esx-1 secretion-associated regulator espr	protein	125	66% helix, 0% strand	P96228
I, K	Esx-1 secretion-associated regulator espr	protein	124	66% helix, 0% strand	P96228
L	Esx-1 secretion-associated regulator espr	protein	129	67% helix, 0% strand	P96228
M	Esx-1 secretion-associated regulator espr	protein	119	66% helix, 0% strand	P96228
O	Esx-1 secretion-associated regulator espr	protein	90	58% helix, 0% strand	P96228
P	Esx-1 secretion-associated regulator espr	protein	92	64% helix, 0% strand	P96228
Q	Esx-1 secretion-associated regulator espr	protein	116	66% helix, 0% strand	P96228
R	Esx-1 secretion-associated regulator espr	protein	123	61% helix, 0% strand	P96228

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.77	0.91	33	empty
2	190	0.77	0.92	33	empty
3	221	0.77	0.91	32	empty
4	223	0.76	0.91	30	empty
5	202	0.76	0.91	32	empty

Interfaces

10 interfaces between chains.

E–F · 2400 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 2399 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 2362 Å² buried · 22 hydrogen bonds · protein-protein
K–L · 2345 Å² buried · 15 hydrogen bonds · protein-protein
G–H · 2344 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 53 modified (engineered).

Compared structures

3R1F · Crystal structure of a key regulator of virulence in 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 P96228
Elsewhere: RCSB PDB 3R1F · PDBe 3R1F · UniProt P96228

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