MolNFT v1 · #15059 · protein
Large scale structural rearrangements of the front loops in monomerised triosephosphate isomerase, as deduced from the comparison of the structural properties of monotim and its point mutation variant monoss
1MSS: “Large scale structural rearrangements of the front loops in monomerised triosephosphate isomerase, as deduced…”. X-ray diffraction. MolNFT v1 #15059 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MSS
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04789
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 242 | — | P04789 |
Compared structures
- 1MSS · Large scale structural rearrangements of the front loops in monomerised triosephosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.97
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.97
- P04789 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P04789) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P04789
- Elsewhere: RCSB PDB 1MSS · PDBe 1MSS · UniProt P04789
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