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Crystal structure of HPOT1V2-ggttagggttag

Analyse Crystal structure of HPOT1V2-ggttagggttag in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KJP
Type: protein + DNA
Length: 304 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protection of telomeres protein 1; 5'-D(*G*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*G)-3'
UniProt: Q9NUX5
Pockets: 5 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protection of telomeres protein 1	protein	293	21% helix, 40% strand	Q9NUX5
B	5'-D(GGPTPTPAPGPGPGPTPTPAPG)-3'	dna	11	—	—

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.50	0.80	28	empty
2	133	0.44	0.76	19	empty
3	93	0.42	0.78	23	empty
4	70	0.37	0.77	15	empty
5	58	0.27	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 1097 Å² buried · 32 hydrogen bonds · protein-nucleic

Compared structures

3KJP · Crystal Structure of hPOT1V2-GGTTAGGGTTAG · the same entry in another collection · chain A against A, TM-score 1.00
Q9NUX5 · AlphaFold monomer V2.0 prediction for protection of telomeres protein 1 (Q9NUX5) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9NUX5
Elsewhere: RCSB PDB 3KJP · PDBe 3KJP · UniProt Q9NUX5

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