Research workbench
Crystal structure of human mitogen-activated protein kinase kinase kinase 3 isoform 2 phox domain at 1.25 a resolution
Analyse Crystal structure of human mitogen-activated protein kinase kinase kinase 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C60
- Type
- protein
- Length
- 85 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human mitogen-activated protein kinase kinase kinase 3 isoform 2
- EC
- 2.7.1.37
- UniProt
- Q99759
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human mitogen-activated protein kinase kinase kinase 3 isoform 2 (EC 2.7.1.37) | protein | 85 | 29% helix, 33% strand | Q99759 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2C60 · crystal structure of human mitogen-activated protein kinase kinase kinase 3 isoform 2… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99759 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase kinase kinase 3… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q99759
- Elsewhere: RCSB PDB 2C60 · PDBe 2C60 · UniProt Q99759
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