MolNFT v1 · #172536 · protein
Enah EVH1 in complex with ac-[2-cl-F]-[prom-2]-[prom-17]-ome
7A5M · Protein enabled homolog: “Enah EVH1 in complex with ac-[2-cl-F]-[prom-2]-[prom-17]-ome”. X-ray diffraction, 4 ligands (2L5, 2L6, R0E). MolNFT v1 #172536 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7A5M
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein enabled homolog
- UniProt
- Q8N8S7
- Ligands
- 2L5, 2L6, R0E, NO3
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein enabled homolog | protein | 112 | 18% helix, 51% strand | Q8N8S7 |
Ligands and binding sites
- 2L5 · 2-chloro-L-phenylalanine · ligand · 2 copies · chains A
- 2L6 · (3s,6r,8as)-5-oxo-1,2,3,8A-tetrahydrospiro[indolizine-6,2'-pyrrolidine]-3-carboxylic acid · ligand · 2 copies · chains A
- R0E · Prom-17 · ligand · 2 copies · chains A
- NO3 · Nitrate ion · ion · chains A
- ACY · Acetic acid · additive · 2 copies · chains A
- MOH · Methanol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q8N8S7
- Elsewhere: RCSB PDB 7A5M · PDBe 7A5M · UniProt Q8N8S7
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