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Crystal structure of hypothetical protein PH1952 from pyrococcus horikoshii OT3

Analyse Crystal structure of hypothetical protein PH1952 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: 1ZJJ
Type: protein
Length: 524 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PH1952
UniProt: O59622
Ligands: MG
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PH1952	protein	261	42% helix, 22% strand	O59622
B	Hypothetical protein PH1952	protein	263	43% helix, 21% strand	O59622

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 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	222	0.63	0.83	36	MG
2	204	0.62	0.83	27	empty
3	94	0.34	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 1201 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1ZJJ · Crystal structure of hypothetical protein PH1952 from Pyrococcus horikoshii OT3 · 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 O59622
Elsewhere: RCSB PDB 1ZJJ · PDBe 1ZJJ · UniProt O59622

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