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Crystal structure of a mutant winged bean chymotrypsin inhibitor protein, N14K.

Analyse Crystal structure of a mutant winged bean chymotrypsin inhibitor protein, N14K. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FMZ
Type: protein
Length: 179 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chymotrypsin inhibitor 3
UniProt: P10822
Ligands: SO4
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chymotrypsin inhibitor 3	protein	179	3% helix, 41% strand	P10822

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.29	0.75	18	empty
2	54	0.27	0.74	13	SO4

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1FMZ · Crystal structure of a mutant winged bean chymotrypsin inhibitor protein, N14K. · the same entry in another collection · chain A against A, TM-score 1.00
P10822 · AlphaFold monomer V2.0 prediction for chymotrypsin inhibitor 3 (P10822) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P10822
Elsewhere: RCSB PDB 1FMZ · PDBe 1FMZ · UniProt P10822

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