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Crystal structure of human P-cadherin (ss-X-dimer-long)
Analyse Crystal structure of human P-cadherin (ss-X-dimer-long) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZMT
- Type
- protein
- Length
- 1,246 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22223
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 214 | — | P22223 |
| B, E | — | protein | 216 | — | P22223 |
| D | — | protein | 213 | — | P22223 |
| F | — | protein | 173 | — | P22223 |
Compared structures
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 P22223
- Elsewhere: RCSB PDB 4ZMT · PDBe 4ZMT · UniProt P22223
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