Research workbench
The C-terminal region of disintegrin modulate its 3D conformation and cooperate with rgd loop in regulating recognitions of integrins
Analyse The C-terminal region of disintegrin modulate its 3D conformation and cooperate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M75
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc METALLOPROTEINASE/DISINTEGRIN
- EC
- 3.4.24.-
- UniProt
- P30403
Structure
solution nmr · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc METALLOPROTEINASE/DISINTEGRIN (EC 3.4.24.-) | protein | 68 | 0% helix, 26% strand | P30403 |
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2M75 · The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD… · the same entry in another collection · chain A against A, TM-score 1.00
- P30403 · AlphaFold monomer V2.0 prediction for zinc METALLOPROTEINASE/DISINTEGRIN (P30403) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 P30403
- Elsewhere: RCSB PDB 2M75 · PDBe 2M75 · UniProt P30403
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