Research workbench
Aspartate transcarbamoylase domain of human cad bound to pala
Analyse Aspartate transcarbamoylase domain of human cad bound to pala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G1N
- Type
- protein
- Length
- 1,837 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cad protein
- EC
- 3.5.2.3, 2.1.3.2
- UniProt
- P27708
- Ligands
- PAL
- Pockets
- 17 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Cad protein (EC 3.5.2.3, 2.1.3.2) | protein | 306 | 42% helix, 16% strand | P27708 |
| E | Cad protein (EC 3.5.2.3, 2.1.3.2) | protein | 307 | 44% helix, 15% strand | P27708 |
Ligands and binding sites
- PAL · N-(phosphonacetyl)-L-aspartic acid · ligand · 6 copies · chains A, B, C, D, E, F
- EDO · 1,2-ethanediol · additive · 2 copies · chains D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.86 | 0.87 | 121 | empty |
| 2 | 1080 | 0.85 | 0.87 | 102 | empty |
| 3 | 82 | 0.76 | 0.99 | 25 | PAL |
| 4 | 82 | 0.76 | 0.99 | 31 | PAL |
| 5 | 70 | 0.73 | 0.98 | 21 | PAL |
Interfaces
9 interfaces between chains.
- E–F · 1187 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1167 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 1128 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1117 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1114 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 P27708
- Elsewhere: RCSB PDB 5G1N · PDBe 5G1N · UniProt P27708
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