Research workbench
Crystal structure of monoclinic rabbit muscle lactate dehydrogenase with four tetramers as the asymmetric unit
Analyse Crystal structure of monoclinic rabbit muscle lactate dehydrogenase with four… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P6U
- Type
- protein
- Length
- 5,296 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lactate dehydrogenase a chain
- EC
- 1.1.1.27
- UniProt
- P13491
- Ligands
- AMP
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | L-lactate dehydrogenase a chain (EC 1.1.1.27) | protein | 331 | 45% helix, 20% strand | P13491 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.89 | 0.91 | 126 | empty |
| 2 | 1128 | 0.89 | 0.91 | 121 | empty |
| 3 | 773 | 0.89 | 0.92 | 110 | empty |
| 4 | 527 | 0.86 | 0.92 | 75 | empty |
| 5 | 303 | 0.82 | 0.93 | 45 | empty |
Interfaces
25 interfaces between chains.
- B–C · 2905 Ų buried · 25 hydrogen bonds · protein-protein
- M–P · 2897 Ų buried · 23 hydrogen bonds · protein-protein
- E–H · 2895 Ų buried · 23 hydrogen bonds · protein-protein
- I–L · 2880 Ų buried · 22 hydrogen bonds · protein-protein
- J–K · 2877 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6P6U · Crystal Structure of Monoclinic Rabbit Muscle Lactate Dehydrogenase with Four Tetramers… · the same entry in another collection · chain P against P, 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 P13491
- Elsewhere: RCSB PDB 6P6U · PDBe 6P6U · UniProt P13491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.