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Crystal structure of pyrococcus horikoshii PH1500

Analyse Crystal structure of pyrococcus horikoshii PH1500 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UZR
Type: protein
Length: 852 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein PH1500
UniProt: O59169
Pockets: 7 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Putative uncharacterized protein PH1500	protein	142	6% helix, 55% strand	O59169

Pockets

7 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	134	0.44	0.76	20	empty
2	171	0.43	0.74	29	empty
3	66	0.41	0.80	14	empty
4	90	0.37	0.75	19	empty
5	59	0.34	0.77	17	empty

Interfaces

6 interfaces between chains.

A–D · 1100 Å² buried · 12 hydrogen bonds · protein-protein
C–F · 1077 Å² buried · 12 hydrogen bonds · protein-protein
B–E · 1044 Å² buried · 11 hydrogen bonds · protein-protein
A–F · 946 Å² buried · 14 hydrogen bonds · protein-protein
C–E · 924 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4UZR · Crystal Structure of Pyrococcus horikoshii Ph1500 · 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 O59169
Elsewhere: RCSB PDB 4UZR · PDBe 4UZR · UniProt O59169

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