MolNFT v1 · #15994 · protein
Structure of signal transduction protein, NMR, minimized average structure
1NLP · C-src: “Structure of signal transduction protein, NMR, minimized average structure”. Solution nmr, 4 ligands (ACE, MN8, MN1). MolNFT v1 #15994 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NLP
- Type
- protein
- Length
- 62 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-src; NL2 (MN8-MN1-plpplp)
- EC
- 2.7.1.112
- UniProt
- P00525
- Ligands
- ACE, MN8, MN1, NH2
Structure
solution nmr · 2 distinct chains · 5% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | C-src (EC 2.7.1.112) | protein | 56 | 5% helix, 45% strand | P00525 |
| N | NL2 (MN8-MN1-plpplp) | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains C
- MN8 · 2-(4-carcoxy-5-isopropylthiazolyl)benzopiperidine · ligand · chains C
- MN1 · 4-carboxypiperidine · ligand · chains C, N
- NH2 · Amino group · ion · chains C, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- C–N · 316 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1NLP · Structure of signal transduction protein, NMR, minimized average structure · the same entry in another collection · chain C against C, 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 P00525
- Elsewhere: RCSB PDB 1NLP · PDBe 1NLP · UniProt P00525
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