MolNFT v1 · #23617 · protein
NMR structure of the complex between nck-2 SH3 domain and pinch-1 LIM4 domain
1U5S · Cytoplasmic protein NCK2: “NMR structure of the complex between nck-2 SH3 domain and pinch-1 LIM4 domain”. Solution nmr, 1 ligand (ZN), 1 pocket (best druggability 0.28). MolNFT v1 #23617 on GenesisL1: 3D structure, binding sites…
- PDB
- 1U5S
- Type
- protein
- Length
- 137 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic protein NCK2; Pinch protein
- UniProt
- O43639, P48059
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.28
Structure
solution nmr · 2 distinct chains · 5% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic protein NCK2 | protein | 71 | 0% helix, 35% strand | O43639 |
| B | Pinch protein | protein | 66 | 11% helix, 26% strand | P48059 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.28 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 241 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1U5S · NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain · the same entry in another collection · chain A against A, TM-score 1.00
- P48059 · AlphaFold monomer V2.0 prediction for lim and senescent cell antigen- like-containing… · a predicted model of the same protein · chain B against A, TM-score 0.79
- O43639 · AlphaFold monomer V2.0 prediction for cytoplasmic protein NCK2 (O43639) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 O43639
- Every structure of UniProt P48059
- Elsewhere: RCSB PDB 1U5S · PDBe 1U5S · UniProt O43639 · UniProt P48059
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