Research workbench
Streptomyces lividans xylan binding domain CBM13 in complex with lactose
Analyse Streptomyces lividans xylan binding domain CBM13 in complex with lactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KNM
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase a
- EC
- 3.2.1.8
- UniProt
- P26514
- Ligands
- BGC, GAL
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase a (EC 3.2.1.8) | protein | 129 | 12% helix, 34% strand | P26514 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1KNM · Streptomyces lividans Xylan Binding Domain cbm13 in Complex with Lactose · the same entry in another collection · chain A against A, TM-score 1.00
- P26514 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P26514) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P26514
- Elsewhere: RCSB PDB 1KNM · PDBe 1KNM · UniProt P26514
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