Research workbench
Integrin ALPHAIIBBETA3-PT25-2 complex
Analyse Integrin ALPHAIIBBETA3-PT25-2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LA4
- Type
- protein
- Length
- 1,052 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P08514, P05106
- Ligands
- NAG, MAN, CA, MG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | — | protein | 116 | — | — |
| L | — | protein | 107 | — | — |
| A | — | protein | 452 | — | P08514 |
| B | — | protein | 377 | — | P05106 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains B, A
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains L, A
- CA · Calcium ion · metal · 6 copies · chains A, B
- MG · Magnesium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LA4 · Integrin AlphaIIbBeta3-PT25-2 Complex · the same entry in another collection · chain H against H, 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 P08514
- Every structure of UniProt P05106
- Elsewhere: RCSB PDB 7LA4 · PDBe 7LA4 · UniProt P08514 · UniProt P05106
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