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Crystal structure of TT1020 from thermus thermophilus HB8

Analyse Crystal structure of TT1020 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V3R
Type: protein
Length: 274 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrogen regulatory protein P-II
UniProt: Q5SM86
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrogen regulatory protein P-II	protein	92	30% helix, 39% strand	Q5SM86
B	Nitrogen regulatory protein P-II	protein	92	30% helix, 39% strand	Q5SM86
C	Nitrogen regulatory protein P-II	protein	90	31% helix, 41% strand	Q5SM86

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	208	0.61	0.81	38	empty
2	167	0.60	0.83	33	empty
3	196	0.56	0.80	31	empty
4	61	0.36	0.78	10	empty

Interfaces

3 interfaces between chains.

B–C · 1183 Å² buried · 16 hydrogen bonds · protein-protein
A–C · 1108 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1085 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1V3R · Crystal structure of TT1020 from Thermus thermophilus HB8 · 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 Q5SM86
Elsewhere: RCSB PDB 1V3R · PDBe 1V3R · UniProt Q5SM86

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