MolNFT v1 · #202251 · protein
AlphaFold monomer V2.0 prediction for lys-gingipain W83 (Q51817)
Q51817: “AlphaFold monomer V2.0 prediction for lys-gingipain W83 (Q51817)”. MolNFT v1 #202251 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q51817
- Type
- protein
- Length
- 1,732 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4BC59faea63ACA4315D24e40823D4B8bF16F1540
- UniProt
- Q51817
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1732 | — | Q51817 |
Compared structures
- 6I9A · Porphyromonas gingivalis gingipain K (kgp) in complex with inhibitor kyt-36 · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 4RBM · Porphyromonas gingivalis gingipain K (Kgp) catalytic and immunoglobulin superfamily-like… · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 4RBM · Porphyromonas gingivalis gingipain K (kgp) catalytic and immunoglobulin superfamily-like… · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 4TKX · Structure of protease · an experimental structure of the same protein · chain A against L, TM-score 0.26
- 4TKX · Structure of Protease · an experimental structure of the same protein · chain A against L, TM-score 0.26
- 5MUN · Structural insight into zymogenic latency of gingipain K from porphyromonas gingivalis. · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 4ITC · Crystal Structure Analysis of the K1 Cleaved Adhesin domain of Lys-gingipain (Kgp) from… · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 4ITC · Crystal structure analysis of the K1 cleaved adhesin domain of lys- gingipain (kgp) from… · an experimental structure of the same protein · chain A against A, TM-score 0.09
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 Q51817
- Elsewhere: UniProt Q51817 · AlphaFold DB Q51817
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