Research workbench

Parvalbumin (MUTATION;D51A, F102W)

Analyse Parvalbumin (MUTATION;D51A, F102W) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B9A
Type: protein
Length: 108 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (parvalbumin)
UniProt: P02618
Ligands: CA

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (parvalbumin)	protein	108	56% helix, 4% strand	P02618

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A

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

Compared structures

1B9A · Parvalbumin (MUTATION;D51A, F102W) · the same entry in another collection · chain A against A, TM-score 1.00
P02618 · AlphaFold monomer V2.0 prediction for parvalbumin beta (P02618) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P02618
Elsewhere: RCSB PDB 1B9A · PDBe 1B9A · UniProt P02618

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