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Crystal structure of PH1033 from pyrococcus horikoshii OT3

Analyse Crystal structure of PH1033 from pyrococcus horikoshii OT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HD9
Type: protein
Length: 145 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UPF0310 protein PH1033
UniProt: O58764
Ligands: CA
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UPF0310 protein PH1033	protein	145	26% helix, 33% strand	O58764

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
CIT · Citric acid · additive · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	234	0.60	0.80	33	CIT, GOL

Compared structures

2HD9 · Crystal structure of PH1033 from Pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
O58764 · AlphaFold monomer V2.0 prediction for UPF0310 protein PH1033 (O58764) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O58764
Elsewhere: RCSB PDB 2HD9 · PDBe 2HD9 · UniProt O58764

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