Research workbench
Structure of hg-nmera, HG(II) complex of the N-terminal domain of TN501 mercuric reductase
Analyse Structure of hg-nmera, HG(II) complex of the N-terminal domain of TN501… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KT3
- Type
- protein
- Length
- 69 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mercuric reductase
- EC
- 1.16.1.1
- UniProt
- P00392
- Ligands
- HG
Structure
solution nmr · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mercuric reductase (EC 1.16.1.1) | protein | 69 | 29% helix, 28% strand | P00392 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2KT3 · Structure of Hg-NmerA, Hg(II) complex of the N-terminal domain of Tn501 Mercuric Reductase · the same entry in another collection · chain A against A, TM-score 1.00
- P00392 · AlphaFold monomer V2.0 prediction for mercuric reductase (P00392) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P00392
- Elsewhere: RCSB PDB 2KT3 · PDBe 2KT3 · UniProt P00392
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