MolNFT v1 · #152649 · protein
The ligand binding domain of MLP24 with proline
6IOS · Methyl-accepting chemotaxis protein: “The ligand binding domain of MLP24 with proline”. X-ray diffraction, 2 ligands (PRO, CA). MolNFT v1 #152649 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IOS
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- A0A0H6VSA0
- Ligands
- PRO, CA
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein | protein | 237 | 36% helix, 29% strand | A0A0H6VSA0 |
Ligands and binding sites
- PRO · Proline · ligand · chains A
- CA · Calcium ion · metal · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IOS · The ligand binding domain of Mlp24 with proline · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0H6VSA0
- Elsewhere: RCSB PDB 6IOS · PDBe 6IOS · UniProt A0A0H6VSA0
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