UniProt P04156
P04156
P04156 (UniProt P04156): 106 experimental structures on GenesisL1, 4 ligands bound. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P04156
- Experimental structures
- 106
- Predicted models
- 0
- Ligands
- 4
Structures
106 records of P04156 in the MolNFT archive: 106 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1FKC | Human prion protein (mutant E200K) fragment 90-231 | solution nmr | A | — | — |
| 1FKC | Human prion protein (mutant E200K) fragment 90-231 | solution nmr | A | — | — |
| 1FO7 | Human prion protein mutant E200K fragment 90-231 | solution nmr | A | — | — |
| 1FO7 | Human prion protein mutant E200K fragment 90-231 | solution nmr | A | — | — |
| 1H0L | Human prion protein 121-230 M166C/E221C | solution nmr | A | — | — |
| 1H0L | Human prion protein 121-230 M166C/E221C | solution nmr | A | — | — |
| 1HJM | Human prion protein at pH 7.0 | solution nmr | A | — | — |
| 1HJM | Human prion protein at pH 7.0 | solution nmr | A | — | — |
| 1HJN | Human prion protein at pH 7.0 | solution nmr | A | — | — |
| 1HJN | Human prion protein at pH 7.0 | solution nmr | A | — | — |
| 1I4M | Crystal structure of the human prion protein reveals a mechanism for oligomerization | x-ray diffraction | A | — | — |
| 1I4M | Crystal structure of the human prion protein reveals a mechanism for oligomerization | x-ray diffraction | A | — | — |
| 1OEH | Human prion protein 61-68 | solution nmr | A | — | — |
| 1OEH | Human prion protein 61-68 | solution nmr | A | — | — |
| 1OEI | Human prion protein 61-84 | solution nmr | A | — | — |
| 1OEI | Human prion protein 61-84 | solution nmr | A | — | — |
| 1QLX | Human prion protein | solution nmr | A | — | — |
| 1QLX | Human prion protein | solution nmr | A | — | — |
| 1QLZ | Human prion protein | solution nmr | A | — | — |
| 1QLZ | Human prion protein | solution nmr | A | — | — |
| 1QM0 | Human prion protein fragment 90-230 | solution nmr | A | — | — |
| 1QM0 | Human prion protein fragment 90-230 | solution nmr | A | — | — |
| 1QM1 | Human prion protein fragment 90-230 | solution nmr | A | — | — |
| 1QM1 | Human prion protein fragment 90-230 | solution nmr | A | — | — |
| 1QM2 | Human prion protein fragment 121-230 | solution nmr | A | — | — |
| 1QM2 | Human prion protein fragment 121-230 | solution nmr | A | — | — |
| 1QM3 | Human prion protein fragment 121-230 | solution nmr | A | — | — |
| 1QM3 | Human prion protein fragment 121-230 | solution nmr | A | — | — |
| 2K1D | NMR Studies of a Pathogenic Mutant (D178N) of the Human Prion Protein | solution nmr | A | — | — |
| 2K1D | NMR studies of a pathogenic mutant (D178N) of the human prion protein | solution nmr | A | — | — |
| 2KUN | Three dimensional structure of HuPrP(90-231 M129 Q212P) | solution nmr | A | — | — |
| 2KUN | Three dimensional structure of HUPRP(90-231 M129 Q212P) | solution nmr | A | — | — |
| 2LBG | Structure of the CHR of the Prion protein in DPC Micelles | solution nmr | A | — | — |
| 2LBG | Structure of the chr of the prion protein in dpc micelles | solution nmr | A | — | — |
| 2LEJ | human prion protein mutant HuPrP(90-231, M129, V210I) | solution nmr | A | — | — |
| 2LEJ | Human prion protein mutant HUPRP(90-231, M129, V210I) | solution nmr | A | — | — |
| 2LFT | Human prion protein with E219K protective polymorphism | solution nmr | A | — | — |
| 2LFT | Human prion protein with E219K protective polymorphism | solution nmr | A | — | — |
| 2LSB | Solution-state NMR structure of the human prion protein | solution nmr | A | — | — |
| 2LSB | Solution-state NMR structure of the human prion protein | solution nmr | A | — | — |
| 2LV1 | Solution-state NMR structure of prion protein mutant V210I at neutral pH | solution nmr | A | — | — |
| 2LV1 | Solution-state NMR structure of prion protein mutant V210I at neutral pH | solution nmr | A | — | — |
| 2M8T | Solution NMR structure of the V209M variant of the human prion protein (residues 90-231) | solution nmr | A | — | — |
| 2M8T | Solution NMR structure of the V209M variant of the human prion protein (residues 90-231) | solution nmr | A | — | — |
| 2W9E | Structure of ICSM 18 (anti-Prp therapeutic antibody) Fab fragment complexed with human Prp fragment… | x-ray diffraction | A | — | — |
| 2W9E | Structure of icsm 18 (anti-prp therapeutic antibody) Fab fragment complexed with human prp fragment… | x-ray diffraction | A | — | — |
| 3HAF | Human prion protein variant V129 domain swapped dimer | x-ray diffraction | A | — | — |
| 3HAF | Human prion protein variant V129 domain swapped dimer | x-ray diffraction | A | — | — |
| 3HAK | Human prion protein variant V129 | x-ray diffraction | A | — | — |
| 3HAK | Human prion protein variant V129 | x-ray diffraction | A | — | — |
| 3HEQ | Human prion protein variant D178N with M129 | x-ray diffraction | A, B | — | — |
| 3HEQ | Human prion protein variant D178N with M129 | x-ray diffraction | A, B | — | — |
| 3HER | Human prion protein variant F198S with V129 | x-ray diffraction | A, B | — | — |
| 3HER | Human prion protein variant F198S with V129 | x-ray diffraction | A, B | — | — |
| 3HES | Human prion protein variant F198S with M129 | x-ray diffraction | A, B | — | — |
| 3HES | Human prion protein variant F198S with M129 | x-ray diffraction | A, B | — | — |
| 3HJ5 | Human prion protein variant V129 domain swapped dimer | x-ray diffraction | A, B | — | — |
| 3HJ5 | Human prion protein variant V129 domain swapped dimer | x-ray diffraction | A, B | — | — |
| 3HJX | Human prion protein variant D178N with V129 | x-ray diffraction | A | — | — |
| 3HJX | Human prion protein variant D178N with V129 | x-ray diffraction | A | — | — |
46 records more on the page itself.
Ligands
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