MolNFT v1 · #24153 · protein
Crystal structure of the VMA1-derived endonuclease with the ligated extein segment
1UM2: “Crystal structure of the VMA1-derived endonuclease with the ligated extein segment”. X-ray diffraction. MolNFT v1 #24153 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UM2
- Type
- protein
- Length
- 850 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P17255
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | P17255 |
| B | — | protein | 419 | — | P17255 |
| C, D | — | protein | 7 | — | P17255 |
Compared structures
- 1UM2 · Crystal Structure of the Vma1-Derived Endonuclease with the Ligated Extein Segment · the same entry in another collection · chain A against A, TM-score 1.00
- P17255 · AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a (P17255) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P17255
- Elsewhere: RCSB PDB 1UM2 · PDBe 1UM2 · UniProt P17255
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