Research workbench
Structure of human slmap fha domain in complex with PMST2
Analyse Structure of human slmap fha domain in complex with PMST2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AR2
- Type
- protein
- Length
- 280 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sarcolemmal membrane-associated protein; Asp-gly-tpo-met-lys-arg
- UniProt
- Q14BN4
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sarcolemmal membrane-associated protein | protein | 134 | 0% helix, 45% strand | Q14BN4 |
| C, D | Asp-gly-tpo-met-lys-arg | protein | 6 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.66 | 0.81 | 51 | empty |
Interfaces
5 interfaces between chains.
- A–B · 502 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 446 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 426 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 141 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 137 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6AR2 · Structure of human SLMAP FHA domain in complex with pMST2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q14BN4 · AlphaFold monomer V2.0 prediction for sarcolemmal membrane-associated protein (Q14BN4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q14BN4
- Elsewhere: RCSB PDB 6AR2 · PDBe 6AR2 · UniProt Q14BN4
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