MolNFT v1 · #116028 · protein

Structure of the C-terminal domain of tnse at 2.85 resolution

5D17 · Transposon TN7 transposition protein tnse: “Structure of the C-terminal domain of tnse at 2.85 resolution”. X-ray diffraction, 19 pockets (best druggability 0.73). MolNFT v1 #116028 on GenesisL1: 3D structure, binding sites and…

PDB: 5D17
Type: protein
Length: 1,894 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transposon TN7 transposition protein tnse
UniProt: P05845
Pockets: 19 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, M	Transposon TN7 transposition protein tnse	protein	159	32% helix, 26% strand	P05845
B, C, E, F, G, I, L	Transposon TN7 transposition protein tnse	protein	158	34% helix, 26% strand	P05845
D, K	Transposon TN7 transposition protein tnse	protein	157	34% helix, 26% strand	P05845
H	Transposon TN7 transposition protein tnse	protein	156	31% helix, 26% strand	P05845

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	936	0.73	0.77	109	empty
2	679	0.70	0.78	70	empty
3	618	0.68	0.77	73	empty
4	267	0.57	0.77	33	empty
5	316	0.56	0.76	45	empty

Interfaces

25 interfaces between chains.

C–D · 682 Å² buried · 13 hydrogen bonds · protein-protein
I–K · 663 Å² buried · 13 hydrogen bonds · protein-protein
A–E · 626 Å² buried · 13 hydrogen bonds · protein-protein
H–M · 620 Å² buried · 13 hydrogen bonds · protein-protein
B–F · 598 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

5D17 · Structure of the C-terminal domain of TnsE at 2.85 resolution · the same entry in another collection · chain M against M, 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 P05845
Elsewhere: RCSB PDB 5D17 · PDBe 5D17 · UniProt P05845

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