MolNFT v1 · #5400 · protein
NMR structure of groes mobile loop residues 19-27 in the synthetic peptide (residues 13-32) bound to groel, 20 structures
1EGS: “NMR structure of groes mobile loop residues 19-27 in the synthetic peptide (residues 13-32) bound to groel…”. Solution nmr, 2 ligands (ACE, NH2). MolNFT v1 #5400 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EGS
- Type
- protein
- Length
- 9 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Groes
- UniProt
- P0A6F9
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Groes | protein | 9 | 0% helix, 0% strand | P0A6F9 |
Ligands and binding sites
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
- 1EGS · NMR structure of groes mobile loop residues 19-27 in the synthetic peptide (residues… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6F9 · AlphaFold monomer V2.0 prediction for 10 kda chaperonin (P0A6F9) · a predicted model of the same protein · chain A against A, TM-score 0.44
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 P0A6F9
- Elsewhere: RCSB PDB 1EGS · PDBe 1EGS · UniProt P0A6F9
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