Research workbench
NMR structure of mouse PAR3-PDZ3 in complex with ve-cadherin C- terminus
Analyse NMR structure of mouse PAR3-PDZ3 in complex with ve-cadherin C- terminus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KOH
- Type
- protein
- Length
- 127 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Partitioning defective 3 homolog; Cadherin-5
- UniProt
- Q99NH2, P55284
Structure
solution nmr · 2 distinct chains · 20% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Partitioning defective 3 homolog | protein | 111 | 23% helix, 39% strand | Q99NH2 |
| B | Cadherin-5 | protein | 16 | 0% helix, 19% strand | P55284 |
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2KOH · NMR structure of mouse Par3-PDZ3 in complex with VE-Cadherin C-terminus · the same entry in another collection · chain A against A, TM-score 1.00
- Q99NH2 · AlphaFold monomer V2.0 prediction for partitioning defective 3 homolog (Q99NH2) · a predicted model of the same protein · chain A against A, TM-score 0.84
- P55284 · AlphaFold monomer V2.0 prediction for cadherin-5 (P55284) · a predicted model of the same protein · chain B against A, TM-score 0.20
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 Q99NH2
- Every structure of UniProt P55284
- Elsewhere: RCSB PDB 2KOH · PDBe 2KOH · UniProt Q99NH2 · UniProt P55284
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