Research workbench
Human histidine decarboxylase complex with histidine methyl ester (hme)
Analyse Human histidine decarboxylase complex with histidine methyl ester (hme) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E1O
- Type
- protein
- Length
- 2,875 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19113
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 478 | — | P19113 |
| C | — | protein | 482 | — | P19113 |
| D, E, F | — | protein | 479 | — | P19113 |
Compared structures
- 4E1O · Human histidine decarboxylase complex with Histidine methyl ester (HME) · the same entry in another collection · chain C against C, TM-score 1.00
- P19113 · AlphaFold monomer V2.0 prediction for histidine decarboxylase (P19113) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P19113
- Elsewhere: RCSB PDB 4E1O · PDBe 4E1O · UniProt P19113
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