Research workbench
Pandda analysis group deposition -- crystal structure of fibrinogen- like globe domain of human tenascin-C in complex with Z2856434840
Analyse Pandda analysis group deposition -- crystal structure of fibrinogen- like globe… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R62
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tenascin C (hexabrachion), isoform CRA_A
- UniProt
- A0A024R884
- Ligands
- RXJ
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tenascin C (hexabrachion), isoform CRA_A | protein | 211 | 21% helix, 32% strand | A0A024R884 |
Ligands and binding sites
- RXJ · 4-(4-methylpiperazin-1-yl)benzonitrile · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5R62 · PanDDA analysis group deposition -- Crystal Structure of FIBRINOGEN-LIKE GLOBE DOMAIN OF… · the same entry in another collection · chain A against A, 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 A0A024R884
- Elsewhere: RCSB PDB 5R62 · PDBe 5R62 · UniProt A0A024R884
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