MolNFT v1 · #22627 · protein
Dissection of the functional role of structural elements of tyrosine- 63 in the catalytic action of human lysozyme
1TAY: “Dissection of the functional role of structural elements of tyrosine- 63 in the catalytic action of human…”. X-ray diffraction. MolNFT v1 #22627 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TAY
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human lysozyme
- EC
- 3.2.1.17
- UniProt
- P61626
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human lysozyme (EC 3.2.1.17) | protein | 130 | 38% helix, 14% strand | P61626 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TAY · Dissection of the functional role of structural elements of tyrosine-63 in the catalytic… · the same entry in another collection · chain A against A, 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 P61626
- Elsewhere: RCSB PDB 1TAY · PDBe 1TAY · UniProt P61626
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