MolNFT v1 · #182242 · protein
Structure of the starch branching enzyme I (bei) complexed with maltododecaose from oryza sativa L
7ML5 · Isoform 2 of 1,4-alpha-glucan-branching enzyme…: “Structure of the starch branching enzyme I (bei) complexed with maltododecaose from oryza sativa L”. X-ray diffraction, 1 ligand (GLC), 7 pockets (best druggability 0.56). MolNFT v1…
- PDB
- 7ML5
- Type
- protein
- Length
- 678 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of 1,4-alpha-glucan-branching enzyme, CHLOROPLASTIC/AMYLOPLASTIC
- EC
- 2.4.1.18
- UniProt
- Q01401
- Ligands
- GLC
- Pockets
- 7 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of 1,4-alpha-glucan-branching enzyme, CHLOROPLASTIC/AMYLOPLASTIC (EC 2.4.1.18) | protein | 678 | 33% helix, 23% strand | Q01401 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 16 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 343 | 0.56 | 0.75 | 37 | empty |
| 2 | 165 | 0.53 | 0.79 | 27 | empty |
| 3 | 70 | 0.45 | 0.82 | 17 | empty |
| 4 | 53 | 0.40 | 0.82 | 17 | empty |
| 5 | 72 | 0.37 | 0.78 | 29 | empty |
Compared structures
- 7ML5 · Structure of the Starch Branching Enzyme I (BEI) complexed with maltododecaose from Oryza… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01401 · AlphaFold monomer V2.0 prediction for 1,4-alpha-glucan-branching enzyme… · 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 Q01401
- Elsewhere: RCSB PDB 7ML5 · PDBe 7ML5 · UniProt Q01401
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