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Structure of pbicp-C in complex with falcipain-2

Analyse Structure of pbicp-C in complex with falcipain-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PNR
Type: protein
Length: 369 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Falcipain 2; Pbicp-C
UniProt: Q9N6S8, Q4YW59
Ligands: CD
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Falcipain 2	protein	240	26% helix, 23% strand	Q9N6S8
B	Pbicp-C	protein	129	2% helix, 53% strand	Q4YW59

Ligands and binding sites

CD · Cadmium ion · metal · 2 copies · chains B, A
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

3 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	161	0.59	0.83	26	empty
2	96	0.47	0.80	15	empty
3	62	0.28	0.73	17	GOL

Interfaces

1 interface between chains.

A–B · 1402 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3PNR · Structure of PbICP-C in complex with falcipain-2 · the same entry in another collection · 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 Q9N6S8
Every structure of UniProt Q4YW59
Elsewhere: RCSB PDB 3PNR · PDBe 3PNR · UniProt Q9N6S8 · UniProt Q4YW59

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