MolNFT v1 · #30029 · protein + DNA
Structure of a synaptic gamma-delta resolvase tetramer covalently linked to two cleaved dnas
1ZR4 · Tcagtgtccgataatttat: “Structure of a synaptic gamma-delta resolvase tetramer covalently linked to two cleaved dnas”. X-ray diffraction, 16 pockets (best druggability 0.78). MolNFT v1 #30029 on GenesisL1: 3D structure, binding sites…
- PDB
- 1ZR4
- Type
- protein + DNA
- Length
- 870 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tcagtgtccgataatttat; Aaa; Ttatcggacactg; Transposon gamma-delta resolvase
- UniProt
- P03012
- Pockets
- 16 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X, J, U, M | Tcagtgtccgataatttat | dna | 19 | — | — |
| Z, I, W, O | Aaa | dna | 3 | — | — |
| Y, K, V, N | Ttatcggacactg | dna | 13 | — | — |
| A, E | Transposon gamma-delta resolvase | protein | 183 | 51% helix, 12% strand | P03012 |
| B, D | Transposon gamma-delta resolvase | protein | 182 | 51% helix, 12% strand | P03012 |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 837 | 0.78 | 0.81 | 95 | empty |
| 2 | 555 | 0.68 | 0.78 | 54 | empty |
| 3 | 346 | 0.65 | 0.80 | 44 | empty |
| 4 | 110 | 0.63 | 0.88 | 17 | empty |
| 5 | 126 | 0.61 | 0.85 | 17 | empty |
Interfaces
31 interfaces between chains.
- J–B · 858 Ų buried · 11 hydrogen bonds · protein-nucleic
- X–A · 828 Ų buried · 9 hydrogen bonds · protein-nucleic
- U–E · 811 Ų buried · 7 hydrogen bonds · protein-nucleic
- M–D · 796 Ų buried · 6 hydrogen bonds · protein-nucleic
- A–B · 683 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1ZR4 · Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently linked to two Cleaved… · the same entry in another collection · chain D against D, 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 P03012
- Elsewhere: RCSB PDB 1ZR4 · PDBe 1ZR4 · UniProt P03012
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