Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RZU

The Crystal Structure 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
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016579biological_processprotein deubiquitination
B0061578molecular_functionK63-linked deubiquitinase activity
B0070536biological_processprotein K63-linked deubiquitination
B0140492molecular_functionmetal-dependent deubiquitinase activity
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0016579biological_processprotein deubiquitination
C0061578molecular_functionK63-linked deubiquitinase activity
C0070536biological_processprotein K63-linked deubiquitination
C0140492molecular_functionmetal-dependent deubiquitinase activity
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0016579biological_processprotein deubiquitination
D0061578molecular_functionK63-linked deubiquitinase activity
D0070536biological_processprotein K63-linked deubiquitination
D0140492molecular_functionmetal-dependent deubiquitinase activity
E0008233molecular_functionpeptidase activity
E0008237molecular_functionmetallopeptidase activity
E0016579biological_processprotein deubiquitination
E0061578molecular_functionK63-linked deubiquitinase activity
E0070536biological_processprotein K63-linked deubiquitination
E0140492molecular_functionmetal-dependent deubiquitinase activity
F0008233molecular_functionpeptidase activity
F0008237molecular_functionmetallopeptidase activity
F0016579biological_processprotein deubiquitination
F0061578molecular_functionK63-linked deubiquitinase activity
F0070536biological_processprotein K63-linked deubiquitination
F0140492molecular_functionmetal-dependent deubiquitinase activity
G0008233molecular_functionpeptidase activity
G0008237molecular_functionmetallopeptidase activity
G0016579biological_processprotein deubiquitination
G0061578molecular_functionK63-linked deubiquitinase activity
G0070536biological_processprotein K63-linked deubiquitination
G0140492molecular_functionmetal-dependent deubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHOH14
AHIS335
AHIS337
AASP348

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

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 3
ChainResidue
BHIS337
BASP348
BHIS335

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 4
ChainResidue
BHIS350
BCYS390
BHIS396
BHIS398

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 5
ChainResidue
CHOH134
CHIS335
CHIS337
CASP348

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 6
ChainResidue
CHIS350
CCYS390
CHIS396
CHIS398

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 7
ChainResidue
DHIS335
DHIS337
DASP348

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 8
ChainResidue
DHOH136
DHIS350
DCYS390
DHIS396
DHIS398

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 9
ChainResidue
EHOH135
EHIS335
EHIS337
EASP348

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 10
ChainResidue
EHOH103
EHIS350
ECYS390
EHIS396
EHIS398

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 11
ChainResidue
FHOH155
FHIS335
FHIS337
FASP348

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 12
ChainResidue
FHIS350
FCYS390
FHIS396
FHIS398

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 13
ChainResidue
GHOH138
GHIS335
GHIS337
GASP348

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN G 14
ChainResidue
GHOH79
GHIS350
GCYS390
GHIS396
GHIS398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
ChainResidueDetails
AHIS335
DHIS335
DHIS337
DASP348
EHIS335
EHIS337
EASP348
FHIS335
FHIS337
FASP348
GHIS335
AHIS337
GHIS337
GASP348
AASP348
BHIS335
BHIS337
BASP348
CHIS335
CHIS337
CASP348

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q96FJ0
ChainResidueDetails
AHIS350
CCYS390
CHIS396
CHIS398
DHIS350
DCYS390
DHIS396
DHIS398
EHIS350
ECYS390
EHIS396
ACYS390
EHIS398
FHIS350
FCYS390
FHIS396
FHIS398
GHIS350
GCYS390
GHIS396
GHIS398
AHIS396
AHIS398
BHIS350
BCYS390
BHIS396
BHIS398
CHIS350

site_idSWS_FT_FI3
Number of Residues7
DetailsSITE: Indirect zinc-binding => ECO:0000250|UniProtKB:Q96FJ0
ChainResidueDetails
AGLU280
BGLU280
CGLU280
DGLU280
EGLU280
FGLU280
GGLU280

site_idSWS_FT_FI4
Number of Residues14
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER243
ESER247
FSER243
FSER247
GSER243
GSER247
ASER247
BSER243
BSER247
CSER243
CSER247
DSER243
DSER247
ESER243

site_idSWS_FT_FI5
Number of Residues7
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516
ChainResidueDetails
ASER245
BSER245
CSER245
DSER245
ESER245
FSER245
GSER245

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon