MolNFT v1 · #90943 · protein

Crystal structure of the C-terminal domain of tetrahymena telomerase protein P65

4EYT · Telomerase associated protein P65: “Crystal structure of the C-terminal domain of tetrahymena telomerase protein P65”. X-ray diffraction, 1 ligand (SO4), 9 pockets (best druggability 0.77). MolNFT v1 #90943 on GenesisL1: 3D…

PDB: 4EYT
Type: protein
Length: 591 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase associated protein P65
UniProt: Q6JXI6
Ligands: SO4
Pockets: 9 · best druggability 0.77

Structure

x-ray diffraction · 5 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomerase associated protein P65	protein	97	35% helix, 30% strand	Q6JXI6
B	Telomerase associated protein P65	protein	99	39% helix, 24% strand	Q6JXI6
C	Telomerase associated protein P65	protein	99	37% helix, 25% strand	Q6JXI6
D	Telomerase associated protein P65	protein	100	34% helix, 29% strand	Q6JXI6
E, F	Telomerase associated protein P65	protein	98	35% helix, 28% strand	Q6JXI6

Ligands and binding sites

SO4 · Sulfate ion · ion · chains B, D

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

Pockets

9 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	854	0.77	0.80	66	SO4
2	889	0.73	0.77	76	empty
3	296	0.63	0.80	27	empty
4	218	0.49	0.75	28	empty
5	119	0.46	0.78	12	empty

Interfaces

10 interfaces between chains.

B–F · 657 Å² buried · 8 hydrogen bonds · protein-protein
A–D · 501 Å² buried · 13 hydrogen bonds · protein-protein
C–E · 387 Å² buried · 7 hydrogen bonds · protein-protein
A–E · 355 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 330 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4EYT · Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65 · 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 Q6JXI6
Elsewhere: RCSB PDB 4EYT · PDBe 4EYT · UniProt Q6JXI6

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