Research workbench
Yeast PEX13 SH3 domain complexed with a peptide from PEX14 at 2.1 a resolution
Analyse Yeast PEX13 SH3 domain complexed with a peptide from PEX14 at 2.1 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V1R
- Type
- protein
- Length
- 156 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P80667, P53112
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 67 | — | P80667 |
| B | — | protein | 68 | — | P80667 |
| P, Q | — | protein | 8 | — | P53112 |
| R | — | protein | 5 | — | P53112 |
Compared structures
- 2V1R · Yeast Pex13 SH3 domain complexed with a peptide from Pex14 at 2.1 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P80667 · AlphaFold monomer V2.0 prediction for peroxisomal membrane protein PAS20 (P80667) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P53112 · AlphaFold monomer V2.0 prediction for peroxisomal membrane protein PEX14 (P53112) · a predicted model of the same protein · chain R against A, TM-score 0.65
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 P80667
- Every structure of UniProt P53112
- Elsewhere: RCSB PDB 2V1R · PDBe 2V1R · UniProt P80667 · UniProt P53112
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