MolNFT v1 · #44963 · protein

1H, 13C, and 15N chemical shift assignments for thymosin alpha 1

2MNQ · Thymosin alpha-1: “1H, 13C, and 15N chemical shift assignments for thymosin alpha 1”. Solution nmr, 1 ligand (ACE). MolNFT v1 #44963 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2MNQ
Type: protein
Length: 28 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymosin alpha-1
UniProt: P06454
Ligands: ACE

Structure

solution nmr · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymosin alpha-1	protein	28	71% helix, 0% strand	P06454

Ligands and binding sites

ACE · Acetyl group · ligand · chains A

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2MNQ · 1H, 13C, and 15N Chemical Shift Assignments for Thymosin alpha 1 · the same entry in another collection · chain A against A, TM-score 1.00
P06454 · AlphaFold monomer V2.0 prediction for prothymosin alpha (P06454) · a predicted model of the same protein · chain A against A, TM-score 0.26

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 P06454
Elsewhere: RCSB PDB 2MNQ · PDBe 2MNQ · UniProt P06454

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