Research workbench
Crystal structure of serine hydroxymethyltransferase, isoform 4 from arabidopsis thaliana (SHM4)
Analyse Crystal structure of serine hydroxymethyltransferase, isoform 4 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q00
- Type
- protein
- Length
- 1,887 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine hydroxymethyltransferase 4
- EC
- 2.1.2.1
- UniProt
- O23254
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase 4 (EC 2.1.2.1) | protein | 471 | 49% helix, 13% strand | O23254 |
| B, C, D | Serine hydroxymethyltransferase 4 (EC 2.1.2.1) | protein | 472 | 49% helix, 13% strand | O23254 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C, D
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.79 | 0.98 | 24 | empty |
| 2 | 82 | 0.78 | 0.99 | 14 | empty |
| 3 | 623 | 0.75 | 0.82 | 66 | empty |
| 4 | 627 | 0.73 | 0.80 | 65 | empty |
| 5 | 571 | 0.72 | 0.80 | 68 | EDO |
Interfaces
6 interfaces between chains.
- A–B · 4885 Ų buried · 65 hydrogen bonds · protein-protein
- C–D · 4883 Ų buried · 66 hydrogen bonds · protein-protein
- B–C · 764 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 741 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 27 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor).
Compared structures
- 7Q00 · Crystal structure of serine hydroxymethyltransferase, isoform 4 from Arabidopsis thaliana… · the same entry in another collection · chain D against D, TM-score 1.00
- O23254 · AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase 4 (O23254) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 O23254
- Elsewhere: RCSB PDB 7Q00 · PDBe 7Q00 · UniProt O23254
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