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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 Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
ChainResidueDetails
AHIS335
AHIS337
AASP348

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q96FJ0
ChainResidueDetails
AHIS350
ACYS390
AHIS396
AHIS398

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Indirect zinc-binding => ECO:0000250|UniProtKB:Q96FJ0
ChainResidueDetails
AALA280

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER243
ASER247

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516
ChainResidueDetails
ASER245

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PDB entries from 2024-06-12

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