MolNFT v1 · #185246 · protein
Cryo-EM structures of human fucosidase FUCA1 reveal insight into substate recognition and catalysis.
7PM4: “Cryo-EM structures of human fucosidase FUCA1 reveal insight into substate recognition and catalysis.”. Electron microscopy, 2 ligands (DFU, NAG). MolNFT v1 #185246 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PM4
- Type
- protein
- Length
- 1,724 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04066
- Ligands
- DFU, NAG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 431 | — | P04066 |
Ligands and binding sites
- DFU · (2S,3R,4S,5R)-2-methylpiperidine-3,4,5-triol · ligand · 4 copies · chains A, B, C, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PM4 · Cryo-EM structures of human fucosidase FucA1 reveal insight into substate recognition and… · the same entry in another collection · chain D against D, TM-score 1.00
- P04066 · AlphaFold monomer V2.0 prediction for tissue alpha-L-fucosidase (P04066) · 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 P04066
- Elsewhere: RCSB PDB 7PM4 · PDBe 7PM4 · UniProt P04066
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