Research workbench
Crystal structure of human M-calpain form I
Analyse Crystal structure of human M-calpain form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KFX
- Type
- protein
- Length
- 816 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P17655, P04632
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 640 | — | P17655 |
| S | — | protein | 176 | — | P04632 |
Compared structures
- 1KFX · Crystal Structure of Human m-Calpain Form I · the same entry in another collection · chain L against L, TM-score 1.00
- P17655 · AlphaFold monomer V2.0 prediction for calpain-2 catalytic subunit (P17655) · a predicted model of the same protein · chain L against A, TM-score 0.93
- P04632 · AlphaFold monomer V2.0 prediction for calpain small subunit 1 (P04632) · a predicted model of the same protein · chain S against A, TM-score 0.88
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 P17655
- Every structure of UniProt P04632
- Elsewhere: RCSB PDB 1KFX · PDBe 1KFX · UniProt P17655 · UniProt P04632
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