Research workbench
Refinement of the C2221 crystal form of oxidized uteroglobin at 1.34 ångströms resolution
Analyse Refinement of the C2221 crystal form of oxidized uteroglobin at 1.34 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UTG
- Type
- protein
- Length
- 70 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uteroglobin
- UniProt
- P02779
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uteroglobin | protein | 70 | 76% helix, 0% strand | P02779 |
Compared structures
- 1UTG · Refinement of the C2221 crystal form of oxidized uteroglobin at 1.34 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P02779 · AlphaFold monomer V2.0 prediction for uteroglobin (P02779) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P02779
- Elsewhere: RCSB PDB 1UTG · PDBe 1UTG · UniProt P02779
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