Research workbench
Solution structure of a complex consisting of HDLG/SAP-97 residues 318-406 and HPV51 oncoprotein E6 residues 141-151
Analyse Solution structure of a complex consisting of HDLG/SAP-97 residues 318-406 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M3M
- Type
- protein
- Length
- 105 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q12959, P26554
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 94 | — | Q12959 |
| B | — | protein | 11 | — | P26554 |
Compared structures
- 2M3M · Solution structure of a complex consisting of hDlg/SAP-97 residues 318-406 and HPV51… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12959 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q12959) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q12959
- Every structure of UniProt P26554
- Elsewhere: RCSB PDB 2M3M · PDBe 2M3M · UniProt Q12959 · UniProt P26554
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