Research workbench
Crystal structure of GIT1 pbd domain in complex with paxillin LD4 motif
Analyse Crystal structure of GIT1 pbd domain in complex with paxillin LD4 motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IUI
- Type
- protein
- Length
- 275 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arf GTPase-activating protein GIT1; Paxillin
- UniProt
- Q9Z272, B4DRY6
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 4 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arf GTPase-activating protein GIT1 | protein | 119 | 79% helix, 0% strand | Q9Z272 |
| B | Arf GTPase-activating protein GIT1 | protein | 113 | 81% helix, 0% strand | Q9Z272 |
| C | Paxillin | protein | 22 | 91% helix, 0% strand | B4DRY6 |
| D | Paxillin | protein | 21 | 86% helix, 0% strand | B4DRY6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.57 | 0.76 | 37 | empty |
| 2 | 65 | 0.40 | 0.80 | 16 | empty |
| 3 | 59 | 0.26 | 0.73 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–C · 831 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 805 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 280 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6IUI · Crystal structure of GIT1 PBD domain in complex with Paxillin LD4 motif · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Z272 · AlphaFold monomer V2.0 prediction for arf GTPase-activating protein GIT1 (Q9Z272) · 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 Q9Z272
- Every structure of UniProt B4DRY6
- Elsewhere: RCSB PDB 6IUI · PDBe 6IUI · UniProt Q9Z272 · UniProt B4DRY6
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