Research workbench

Prtc methionine mutants: M226I

Analyse Prtc methionine mutants: M226I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HB2
Type: protein
Length: 462 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secreted protease C
EC: 3.4.24.-
UniProt: P16317
Ligands: CA, ZN, CL
Pockets: 4 · best druggability 0.51

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	Secreted protease C (EC 3.4.24.-)	protein	462	19% helix, 24% strand	P16317

Ligands and binding sites

CA · Calcium ion · metal · 7 copies · chains P
ZN · Zinc ion · metal · chains P
CL · Chloride ion · ion · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.51	0.80	22	empty
2	156	0.51	0.79	32	empty
3	117	0.38	0.74	25	empty
4	58	0.31	0.76	15	empty

Compared structures

3HB2 · PrtC methionine mutants: M226I · 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 3HB2 · PDBe 3HB2 · UniProt P16317

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