3RZU: Catalytic Domain of AMSH
The Crystal Structure of the Catalytic Domain of AMSH. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Oct 2011.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 9,740
- Mol. weight
- 145.23 kDa
- Ligands
- ZN
- Released
- 19 Oct 2011
Explore 3RZU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3RZU contains 41 α-helices and 83 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 5 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 251 | 1 | 1 |
| β-strand | 254 | 1 | 1 |
| β-strand | 256-260 | 5 | 2 |
| α-helix | 263-276 | 14 | |
| β-strand | 282-289 | 8 | 2 |
| β-strand | 293-301 | 9 | 2 |
| β-strand | 304-306 | 3 | 3 |
| β-strand | 311-313 | 3 | 3 |
| α-helix | 316-324 | 9 | |
| β-strand | 329-336 | 8 | 2 |
| α-helix | 346-358 | 13 | |
| β-strand | 363-368 | 6 | 2 |
| α-helix | 369-371 | 3 | |
| β-strand | 373-379 | 7 | 2 |
| α-helix | 381-389 | 9 | |
| β-strand | 405-407 | 3 | 2 |
| β-strand | 411-414 | 4 | 2 |
| β-strand | 419-422 | 4 | 2 |
Chain B: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 250-251 | 2 | 4 |
| β-strand | 254-255 | 2 | 4 |
| β-strand | 256-260 | 5 | 3 |
| α-helix | 263-270 | 8 | |
| α-helix | 272-276 | 5 | |
| β-strand | 282-289 | 8 | 3 |
| β-strand | 293-301 | 9 | 3 |
| β-strand | 304-306 | 3 | 5 |
| β-strand | 311-313 | 3 | 5 |
| α-helix | 317-324 | 8 | |
| β-strand | 329-336 | 8 | 3 |
| α-helix | 346-358 | 13 | |
| β-strand | 363-368 | 6 | 3 |
| α-helix | 369-371 | 3 | |
| β-strand | 373-379 | 7 | 3 |
| α-helix | 381-389 | 9 | |
| β-strand | 405-407 | 3 | 3 |
| β-strand | 411-414 | 4 | 3 |
| β-strand | 419-422 | 4 | 3 |
Chain C: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 249 | 1 | 6 |
| β-strand | 255 | 1 | 6 |
| β-strand | 256-260 | 5 | 7 |
| α-helix | 263-270 | 8 | |
| α-helix | 272-276 | 5 | |
| β-strand | 282-289 | 8 | 7 |
| β-strand | 293-301 | 9 | 7 |
| β-strand | 304-306 | 3 | 2 |
| β-strand | 311-313 | 3 | 2 |
| α-helix | 318-324 | 7 | |
| β-strand | 329-336 | 8 | 7 |
| α-helix | 346-358 | 13 | |
| β-strand | 363-368 | 6 | 7 |
| α-helix | 369-371 | 3 | |
| β-strand | 373-379 | 7 | 7 |
| α-helix | 381-389 | 9 | |
| β-strand | 405-407 | 3 | 7 |
| β-strand | 411-414 | 4 | 7 |
| β-strand | 419-422 | 4 | 7 |
Chains D, E and F: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 256-260 | 5 | 5 |
| α-helix | 263-270 | 8 | |
| α-helix | 272-276 | 5 | |
| β-strand | 282-289 | 8 | 5 |
| β-strand | 293-301 | 9 | 5 |
| β-strand | 304-306 | 3 | 8 |
| β-strand | 311-313 | 3 | 8 |
| α-helix | 316-324 | 9 | |
| β-strand | 329-336 | 8 | 5 |
| α-helix | 346-358 | 13 | |
| β-strand | 363-368 | 6 | 5 |
| α-helix | 369-371 | 3 | |
| β-strand | 373-379 | 7 | 5 |
| α-helix | 381-389 | 9 | |
| β-strand | 405-407 | 3 | 5 |
| β-strand | 411-414 | 4 | 5 |
| β-strand | 419-422 | 4 | 5 |
Chain G: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 256-260 | 5 | 12 |
| α-helix | 263-270 | 8 | |
| α-helix | 272-275 | 4 | |
| β-strand | 282-289 | 8 | 12 |
| β-strand | 293-301 | 9 | 12 |
| β-strand | 304-306 | 3 | 7 |
| β-strand | 311-313 | 3 | 7 |
| α-helix | 317-324 | 8 | |
| β-strand | 329-336 | 8 | 12 |
| α-helix | 346-358 | 13 | |
| β-strand | 363-368 | 6 | 12 |
| α-helix | 369-371 | 3 | |
| β-strand | 373-379 | 7 | 12 |
| α-helix | 381-389 | 9 | |
| β-strand | 405-407 | 3 | 12 |
| β-strand | 411-414 | 4 | 12 |
| β-strand | 419-422 | 4 | 12 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| STAM-binding protein | A, B, C, D, E, F, G | protein | 187 | Homo sapiens | O95630 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>3RZU_1 STAM-binding protein (chains A, B, C, D, E, F, G)
GPLGSSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTIT
HVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQM
MLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRA
VTITDLR
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 14 |
Primary citation
Structural and Thermodynamic Comparison of the Catalytic Domain of AMSH and AMSH-LP: Nearly Identical Fold but Different Stability. Davies, C.W., Paul, L.N., Kim, M.I. et al. J Mol Biol (2011) 413:416-429. DOI 10.1016/j.jmb.2011.08.029 · PubMed
Other PDB entries of the same protein (UniProt O95630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3RZV 1.67 Å, The Crystal Structure of a E280A Mutant of the Catalytic Domain of AMSH
- 2XZE 1.75 Å, Structural basis for AMSH-ESCRT-III CHMP3 interaction
- 9LE4 2.6 Å, Crystal structure of the MIT-CD complex of STAMBP
- 5IXF Solution structure of the STAM2 SH3 with AMSH derived peptide complex
Browse structure collections
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