Research workbench

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors

Analyse Structural basis of the resistance of an insect carboxypeptidase to plant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C1C
Type: protein
Length: 623 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxypeptidase B
EC: 3.4.17.2
Ligands: ZN, Y1
Pockets: 4 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxypeptidase B (EC 3.4.17.2)	protein	312	39% helix, 17% strand	—
B	Carboxypeptidase B (EC 3.4.17.2)	protein	311	39% helix, 17% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
Y1 · Yttrium ion · metal · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.54	0.84	21	empty
2	72	0.53	0.86	15	empty
3	99	0.52	0.83	23	empty
4	69	0.51	0.85	14	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2C1C · Structural basis of the resistance of an insect carboxypeptidase to plant protease… · 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
Elsewhere: RCSB PDB 2C1C · PDBe 2C1C

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.