MolNFT v1 · #26693 · protein

Crystal structure of PH1933 from pyrococcus horikoshii OT3

1WWZ · Hypothetical protein PH1933: “Crystal structure of PH1933 from pyrococcus horikoshii OT3”. X-ray diffraction, 1 ligand (ACO), 3 pockets (best druggability 0.68). MolNFT v1 #26693 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1WWZ
Type: protein
Length: 314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PH1933
UniProt: O59596
Ligands: ACO
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PH1933	protein	157	40% helix, 35% strand	O59596
B	Hypothetical protein PH1933	protein	157	43% helix, 36% strand	O59596

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.68	0.79	48	ACO
2	514	0.65	0.76	54	ACO
3	248	0.61	0.80	35	empty

Interfaces

1 interface between chains.

A–B · 689 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1WWZ · Crystal structure of PH1933 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 O59596
Elsewhere: RCSB PDB 1WWZ · PDBe 1WWZ · UniProt O59596

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