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3RZV

The Crystal Structure of a E280A Mutant of the Catalytic Domain of AMSH

Functional Information from GO Data
ChainGOidnamespacecontents
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016579biological_processprotein deubiquitination
A0061578molecular_functionK63-linked deubiquitinase activity
A0070536biological_processprotein K63-linked deubiquitination
A0140492molecular_functionmetal-dependent deubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AASP309
AHIS335
AHIS337
AASP348

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AHIS350
ACYS390
AHIS396
AHIS398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues131
DetailsDomain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsMotif: {"description":"JAMM motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q96FJ0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Indirect zinc-binding","evidences":[{"source":"UniProtKB","id":"Q96FJ0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11483516","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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