MolNFT v1 · #8649 · protein
The role of conserved amino acids in the cleft of the C-terminal family 22 carbohydrate binding module of clostridium thermocellum XYN10B in ligand binding
1H6X · Endo-1,4-beta-xylanase Y: “The role of conserved amino acids in the cleft of the C-terminal family 22 carbohydrate binding module of…”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #8649 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1H6X
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase Y
- UniProt
- P51584
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase Y | protein | 159 | 0% helix, 52% strand | P51584 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1H6X · The role of conserved amino acids in the cleft of the C-terminal family 22 carbohydrate… · the same entry in another collection · chain A against A, TM-score 1.00
- P51584 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Y (P51584) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P51584
- Elsewhere: RCSB PDB 1H6X · PDBe 1H6X · UniProt P51584
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.