Research workbench

Prtc from erwinia chrysanthemi: E189A mutant

Analyse Prtc from erwinia chrysanthemi: E189A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K7Q
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
Pockets: 4 · best druggability 0.52

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	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 A
ZN · Zinc ion · metal · chains A

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	133	0.52	0.81	21	empty
2	147	0.52	0.80	28	empty
3	108	0.36	0.74	22	empty
4	64	0.31	0.75	16	empty

Compared structures

1K7Q · PrtC from Erwinia chrysanthemi: E189A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P16317 · AlphaFold monomer V2.0 prediction for serralysin C (P16317) · a predicted model of the same protein · 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 P16317
Elsewhere: RCSB PDB 1K7Q · PDBe 1K7Q · UniProt P16317

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