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Prtc from erwinia chrysanthemi

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

PDB: 1K7G
Type: protein
Length: 455 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, PO4
Pockets: 5 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Secreted protease C (EC 3.4.24.-)	protein	455	18% helix, 24% strand	P16317

Ligands and binding sites

CA · Calcium ion · metal · 7 copies · chains A
ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.55	0.81	23	empty
2	155	0.48	0.77	28	PO4
3	94	0.34	0.74	23	empty
4	55	0.30	0.75	14	empty
5	61	0.28	0.74	15	empty

Compared structures

1K7G · PrtC from Erwinia chrysanthemi · 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 1K7G · PDBe 1K7G · UniProt P16317

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