MolNFT v1 · #116786 · protein

Crystal structure of tetrahymena P19

5DOF · Telomerase-associated protein 19: “Crystal structure of tetrahymena P19”. X-ray diffraction, 10 pockets (best druggability 0.61). MolNFT v1 #116786 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5DOF
Type: protein
Length: 612 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase-associated protein 19
UniProt: D2CVN7
Pockets: 10 · best druggability 0.61

Structure

x-ray diffraction · 4 distinct chains · 31% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomerase-associated protein 19	protein	154	31% helix, 31% strand	D2CVN7
B	Telomerase-associated protein 19	protein	151	30% helix, 31% strand	D2CVN7
C	Telomerase-associated protein 19	protein	151	31% helix, 32% strand	D2CVN7
D	Telomerase-associated protein 19	protein	156	31% helix, 31% strand	D2CVN7

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	400	0.61	0.77	58	empty
2	217	0.58	0.80	31	empty
3	164	0.49	0.77	20	empty
4	201	0.46	0.75	27	empty
5	118	0.42	0.76	19	empty

Interfaces

5 interfaces between chains.

B–D · 1705 Å² buried · 32 hydrogen bonds · protein-protein
A–C · 1686 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 900 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 766 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 136 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

5DOF · Crystal structure of Tetrahymena p19 · the same entry in another collection · chain D against D, TM-score 1.00
D2CVN7 · AlphaFold monomer V2.0 prediction for telomerase-associated protein of 19 kda (D2CVN7) · a predicted model of the same protein · chain B against A, TM-score 0.25

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 D2CVN7
Elsewhere: RCSB PDB 5DOF · PDBe 5DOF · UniProt D2CVN7

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