3RZV: E280A Mutant of the Catalytic Domain of AMSH

The Crystal Structure of a E280A Mutant of the Catalytic Domain of AMSH. Determined by X-ray diffraction at 1.67 Å resolution. Released 19 Oct 2011.

Method
X-ray diffraction
Resolution
1.67 Å
Organism
Homo sapiens
Chains
1
Atoms
1,633
Mol. weight
23.22 kDa
Ligands
ZN
Released
19 Oct 2011

Explore 3RZV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RZV contains 6 α-helices and 13 β-strands across 1 chain. 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: 6 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix247-2504
β-strand25111
β-strand25411
β-strand257-26042
α-helix263-27614
β-strand282-29092
β-strand293-30192
β-strand304-30633
β-strand311-31333
α-helix316-32611
α-helix3281
β-strand329-33682
α-helix346-35813
β-strand363-36862
β-strand373-37972
α-helix381-3899
β-strand405-40732
β-strand411-41442
β-strand419-42242

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
STAM-binding proteinAprotein211Homo sapiensO95630 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3RZV_1 STAM-binding protein (chains A)
GPLGSSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASA
NTARGVATCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGW
IHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQK
GFHPHSKDPPLFCSCSHVTVVDRAVTITDLR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

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:

Browse structure collections

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