MolNFT v1 · #184029 · protein

Cpr-C4 - a conserved novel protease from the candidate phyla radiation

7OB6: “Cpr-C4 - a conserved novel protease from the candidate phyla radiation”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.73). MolNFT v1 #184029 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7OB6
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cpr-C4
Ligands: ZN
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cpr-C4	protein	222	40% helix, 20% strand	—
B	Cpr-C4	protein	213	41% helix, 19% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.73	0.98	19	empty
2	205	0.69	0.86	36	empty
3	293	0.61	0.79	34	empty
4	300	0.60	0.78	35	empty
5	61	0.33	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 1724 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

7OB6 · CPR-C4 - a conserved novel protease from the Candidate Phyla Radiation · 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
Elsewhere: RCSB PDB 7OB6 · PDBe 7OB6

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