Research workbench

Yersinia Pestis Plasminogen Activator Pla (Native)

Analyse Yersinia Pestis Plasminogen Activator Pla (Native) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X56
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: YERSINIA PESTIS
Molecule: COAGULASE/FIBRINOLYSIN
EC: 3.4.23.48
UniProt: P17811
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 2% helix, 78% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	COAGULASE/FIBRINOLYSIN (EC 3.4.23.48)	protein	272	2% helix, 78% strand	P17811

Ligands and binding sites

C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 18 copies · chains A

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

Pockets

3 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	185	0.81	0.96	32	empty
2	152	0.51	0.79	25	C8E
3	97	0.38	0.76	22	empty

Compared structures

2X56 · Yersinia pestis plasminogen activator pla (native) · the same entry in another collection · chain A against A, TM-score 1.00
P17811 · AlphaFold monomer V2.0 prediction for COAGULASE/FIBRINOLYSIN (P17811) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P17811
Elsewhere: RCSB PDB 2X56 · PDBe 2X56 · UniProt P17811

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