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Crystal structure of serine hydroxymethyltransferase from mycobacterium tuberculosis with bound plp forming a schiff base with substrate serine in one monomer and plp forming a schiff base with product glycine in the other monomer
Analyse Crystal structure of serine hydroxymethyltransferase from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ULD
- Type
- protein
- Length
- 858 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0T9NP28
- Ligands
- PLP
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 430 | — | A0A0T9NP28 |
| B | — | protein | 428 | — | A0A0T9NP28 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ULD · Crystal structure of serine hydroxymethyltransferase from Mycobacterium tuberculosis with… · 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 A0A0T9NP28
- Elsewhere: RCSB PDB 6ULD · PDBe 6ULD · UniProt A0A0T9NP28
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