MolNFT v1 · #33258 · protein

Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell

2CF4 · Protein PH0519: “Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell”. X-ray diffraction, 1 ligand (CO), 1 pocket (best druggability 0.29). MolNFT v1 #33258 on GenesisL1: 3D structure…

PDB: 2CF4
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein PH0519
EC: 3.4.11.-
UniProt: O58255
Ligands: CO
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein PH0519 (EC 3.4.11.-)	protein	330	22% helix, 23% strand	O58255

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.29	0.74	16	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

2CF4 · Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large… · 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 O58255
Elsewhere: RCSB PDB 2CF4 · PDBe 2CF4 · UniProt O58255

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