Research workbench
B12-dependent radical SAM methyltransferase, MMP10 with [4FE-4S] cluster, cobalamin, S-adenosyl-L-methionine, and peptide bound.
Analyse B12-dependent radical SAM methyltransferase, MMP10 with [4FE-4S] cluster… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QBS
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A832SFM5
- Ligands
- SF4, COB, FE, NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 412 | — | A0A832SFM5 |
| B | — | protein | 8 | — | — |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- COB · Co-methylcobalamin · ligand · chains A, B
- FE · Fe (III) ion · metal · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7QBS · B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin… · the same entry in another collection · chain B against B, 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 A0A832SFM5
- Elsewhere: RCSB PDB 7QBS · PDBe 7QBS · UniProt A0A832SFM5
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