Research workbench
Crystal structure of GIT1/PAXILLIN complex
Analyse Crystal structure of GIT1/PAXILLIN complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JMU
- Type
- protein
- Length
- 295 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arf GTPase-activating protein GIT1; Paxillin
- UniProt
- Q68FF6, Q8VI36
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arf GTPase-activating protein GIT1 | protein | 127 | 73% helix, 2% strand | Q68FF6 |
| C | Paxillin | protein | 21 | 81% helix, 0% strand | Q8VI36 |
| D | Paxillin | protein | 20 | 80% helix, 0% strand | Q8VI36 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.51 | 0.75 | 28 | empty |
| 2 | 236 | 0.51 | 0.75 | 35 | empty |
Interfaces
3 interfaces between chains.
- B–D · 834 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 833 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 350 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6JMU · Crystal structure of GIT1/Paxillin complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q68FF6 · AlphaFold monomer V2.0 prediction for arf GTPase-activating protein GIT1 (Q68FF6) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q8VI36 · AlphaFold monomer V2.0 prediction for paxillin (Q8VI36) · a predicted model of the same protein · chain C against A, TM-score 0.60
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 Q68FF6
- Every structure of UniProt Q8VI36
- Elsewhere: RCSB PDB 6JMU · PDBe 6JMU · UniProt Q68FF6 · UniProt Q8VI36
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