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Crystal structure of HPOT1V2-DTRUD(AGGGTTAG)

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

PDB: 3KJO
Type: protein + DNA
Length: 301 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protection of telomeres protein 1; DNA/RNA (5'-D(*T)-R(P*U)-D(P*AP*GP*GP*GP*TP*TP*AP*G)-3'…
UniProt: Q9NUX5
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protection of telomeres protein 1	protein	291	20% helix, 41% strand	Q9NUX5
B	DNA/RNA (5'-D(T)-R(PU)-D(PAPGPGPGPTPTPAPG)-3')	dna	10	—	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	351	0.62	0.78	44	empty
2	90	0.49	0.82	19	empty
3	53	0.29	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1115 Å² buried · 27 hydrogen bonds · protein-nucleic

Compared structures

3KJO · Crystal Structure of hPOT1V2-dTrUd(AGGGTTAG) · 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 0.96

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 3KJO · PDBe 3KJO · UniProt Q9NUX5

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