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2ZNV

Crystal structure of human AMSH-LP DUB domain in complex with Lys63-linked ubiquitin dimer

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
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0016579biological_processprotein deubiquitination
D0061578molecular_functionK63-linked deubiquitinase activity
D0070536biological_processprotein K63-linked deubiquitination
D0140492molecular_functionmetal-dependent deubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS362
ACYS402
AHIS408
AHIS410

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 2
ChainResidue
DHIS362
DCYS402
DHIS408
DHIS410

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 2
ChainResidue
ASER366
ASER400
AHOH528
BGLY35
BPRO37
BGLN40
AHIS362

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 77
ChainResidue
AHOH439
BTHR7
BLEU8
BLEU69
BVAL70
BLEU71

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 3
ChainResidue
CASP32
DVAL359
DLYS405
DGLY406
DPHE407
DHOH610
EARG74

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
CARG54
CARG72
FARG54
FARG72
DHIS349
DASP360

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
CHIS68
FHIS68
AHIS408
AHIS410
DHIS362
DCYS402
DHIS408
DHIS410

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48
ChainResidueDetails
CSER65
FSER65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000250|UniProtKB:P0CG48
ChainResidueDetails
CGLY76
FGLY76

site_idSWS_FT_FI5
Number of Residues14
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
ChainResidueDetails
CLYS6
FLYS27
FLYS29
FLYS33
FLYS48
FLYS63
CLYS11
CLYS27
CLYS29
CLYS33
CLYS48
CLYS63
FLYS6
FLYS11

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
ChainResidueDetails
CGLY76
FGLY76

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PDB entries from 2024-11-06

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