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Backbone 1H, 13C, and 15N chemical shift assignments for bovine apo calbindin

Analyse Backbone 1H, 13C, and 15N chemical shift assignments for bovine apo calbindin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MAZ
Type: protein
Length: 75 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein S100-G
UniProt: P02633
Pockets: 2 · best druggability 0.63

Structure

solution nmr · 1 distinct chain · 56% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein S100-G	protein	75	56% helix, 5% strand	P02633

Pockets

2 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	234	0.63	0.81	21	empty
2	50	0.31	0.77	14	empty

Compared structures

2MAZ · Backbone 1H, 13C, and 15N Chemical Shift Assignments for Bovine Apo Calbindin · the same entry in another collection · chain A against A, TM-score 1.00
P02633 · AlphaFold monomer V2.0 prediction for protein S100-G (P02633) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P02633
Elsewhere: RCSB PDB 2MAZ · PDBe 2MAZ · UniProt P02633

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