Research workbench
Crystal structure of arabidopsis TEM1 AP2 domain
Analyse Crystal structure of arabidopsis TEM1 AP2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ET4
- Type
- protein + DNA
- Length
- 499 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AP2/ERF and B3 domain-containing transcription repressor TEM1; DNA (12-mer)
- UniProt
- Q9C6M5
- Pockets
- 12 · best druggability 0.53
Structure
x-ray diffraction · 8 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AP2/ERF and B3 domain-containing transcription repressor TEM1 | protein | 102 | 40% helix, 18% strand | Q9C6M5 |
| B, F, L | DNA (12-mer) | dna | 12 | — | — |
| C, E | DNA (12-mer) | dna | 11 | — | — |
| D | AP2/ERF and B3 domain-containing transcription repressor TEM1 | protein | 104 | 44% helix, 17% strand | Q9C6M5 |
| G | AP2/ERF and B3 domain-containing transcription repressor TEM1 | protein | 99 | 46% helix, 18% strand | Q9C6M5 |
| H, K | DNA (12-mer) | dna | 12 | — | — |
| I | DNA (12-mer) | dna | 11 | — | — |
| J | AP2/ERF and B3 domain-containing transcription repressor TEM1 | protein | 101 | 45% helix, 20% strand | Q9C6M5 |
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.53 | 0.85 | 20 | empty |
| 2 | 62 | 0.53 | 0.87 | 17 | empty |
| 3 | 88 | 0.43 | 0.80 | 15 | empty |
| 4 | 108 | 0.42 | 0.78 | 22 | empty |
| 5 | 81 | 0.38 | 0.77 | 15 | empty |
Interfaces
26 interfaces between chains.
- K–L · 600 Ų buried · 50 hydrogen bonds · nucleic-nucleic
- H–I · 532 Ų buried · 59 hydrogen bonds · nucleic-nucleic
- B–C · 505 Ų buried · 41 hydrogen bonds · nucleic-nucleic
- E–F · 503 Ų buried · 45 hydrogen bonds · nucleic-nucleic
- A–C · 499 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 7ET4 · Crystal structure of Arabidopsis TEM1 AP2 domain · the same entry in another collection · chain L against L, TM-score 1.00
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 Q9C6M5
- Elsewhere: RCSB PDB 7ET4 · PDBe 7ET4 · UniProt Q9C6M5
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