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The METZINCIN'S methionine: prtc M226L mutant

Analyse The METZINCIN'S methionine: prtc M226L mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GO8
Type: protein
Length: 460 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease C
UniProt: P16317
Ligands: CA, ZN, PO4
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	Protease C	protein	460	19% helix, 24% strand	P16317

Ligands and binding sites

CA · Calcium ion · metal · 7 copies · chains P
ZN · Zinc ion · metal · chains P
PO4 · Phosphate ion · ion · chains P

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.55	0.82	22	empty
2	147	0.48	0.78	28	ZN, PO4
3	106	0.37	0.75	22	empty
4	70	0.33	0.75	17	empty

Compared structures

1GO8 · The metzincin's methionine: PrtC M226L mutant · the same entry in another collection · chain P against P, TM-score 1.00
P16317 · AlphaFold monomer V2.0 prediction for serralysin C (P16317) · a predicted model of the same protein · chain P 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 P16317
Elsewhere: RCSB PDB 1GO8 · PDBe 1GO8 · UniProt P16317

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