Research workbench
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADASE II) in complex with a transition state analog of glu-glu
Analyse The high resolution structure of human glutamate carboxypeptidase III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FED
- Type
- protein
- Length
- 691 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y3Q0
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 691 | — | Q9Y3Q0 |
Compared structures
- 3FED · The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y3Q0 · AlphaFold monomer V2.0 prediction for N-acetylated-alpha-linked acidic dipeptidase 2… · 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 Q9Y3Q0
- Elsewhere: RCSB PDB 3FED · PDBe 3FED · UniProt Q9Y3Q0
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