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Crystal structure of an AIG2-like protein (A2LD1, ggact, MGC7867) from mus musculus at 1.90 a resolution
Analyse Crystal structure of an AIG2-like protein (A2LD1, ggact, MGC7867) from mus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VKB
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q923B0
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 147 | 15% helix, 36% strand | Q923B0 |
Ligands and binding sites
- FMT · Formic acid · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1VKB · Crystal structure of an aig2-like protein (a2ld1, ggact, mgc7867) from mus musculus at… · the same entry in another collection · chain A against A, TM-score 1.00
- Q923B0 · AlphaFold monomer V2.0 prediction for gamma- glutamylaminecyclotransferase (Q923B0) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q923B0
- Elsewhere: RCSB PDB 1VKB · PDBe 1VKB · UniProt Q923B0
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