Research workbench
Human PA200-20S complex
Analyse Human PA200-20S complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KWY
- Type
- protein
- Length
- 7,968 residues
- Chains
- 29
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25787, P25789, O14818, P28066, P25786, P25788, P60900, Q99436, P49720, P49721, P28074, P20618, P28070, P28072, Q14997
- Ligands
- K0W, IHP
Structure
electron microscopy · 24 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 215 | — | P25787 |
| B | — | protein | 212 | — | P25789 |
| C | — | protein | 212 | — | O14818 |
| D | — | protein | 227 | — | P28066 |
| E | — | protein | 240 | — | P25786 |
| F | — | protein | 245 | — | P25788 |
| G | — | protein | 237 | — | P60900 |
| H, V | — | protein | 220 | — | Q99436 |
| I, W | — | protein | 204 | — | P49720 |
| J, X | — | protein | 196 | — | P49721 |
| K | — | protein | 201 | — | P28074 |
| L, Z | — | protein | 213 | — | P20618 |
| M, a | — | protein | 216 | — | P28070 |
| N | — | protein | 202 | — | P28072 |
| O | — | protein | 230 | — | P25787 |
| P | — | protein | 247 | — | P25789 |
| Q | — | protein | 234 | — | O14818 |
| R | — | protein | 233 | — | P28066 |
| S | — | protein | 238 | — | P25786 |
| T | — | protein | 240 | — | P25788 |
| U | — | protein | 244 | — | P60900 |
| Y | — | protein | 199 | — | P28074 |
| b | — | protein | 203 | — | P28072 |
| c | — | protein | 1811 | — | Q14997 |
Ligands and binding sites
- K0W · [(1~{S},2~{R},3~{R},4~{S},5~{S},6~{R})-2-[oxidanyl(phosphonooxy)phosphoryl]oxy-3,4,5,6-tetraphosphonooxy-cyclohexyl] phosphono hydrogen phosphate · ligand · chains c
- IHP · Inositol hexakisphosphate · ligand · chains c
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KWY · human PA200-20S complex · the same entry in another collection · chain K against K, 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 P25787
- Every structure of UniProt P25789
- Every structure of UniProt O14818
- Every structure of UniProt P28066
- Every structure of UniProt P25786
- Every structure of UniProt P25788
- Every structure of UniProt P60900
- Every structure of UniProt Q99436
- Every structure of UniProt P49720
- Every structure of UniProt P49721
- Every structure of UniProt P28074
- Every structure of UniProt P20618
- Every structure of UniProt P28070
- Every structure of UniProt P28072
- Every structure of UniProt Q14997
- Elsewhere: RCSB PDB 6KWY · PDBe 6KWY · UniProt P25787 · UniProt P25789 · UniProt O14818 · UniProt P28066 · UniProt P25786 · UniProt P25788 · UniProt P60900 · UniProt Q99436 · UniProt P49720 · UniProt P49721 · UniProt P28074 · UniProt P20618 · UniProt P28070 · UniProt P28072 · UniProt Q14997
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