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3IHR

Crystal Structure of Uch37

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0000723biological_processtelomere maintenance
A0003723molecular_functionRNA binding
A0004843molecular_functioncysteine-type deubiquitinase activity
A0004866molecular_functionendopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006275biological_processregulation of DNA replication
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006310biological_processDNA recombination
A0006338biological_processchromatin remodeling
A0006508biological_processproteolysis
A0006511biological_processubiquitin-dependent protein catabolic process
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0021670biological_processlateral ventricle development
A0030901biological_processmidbrain development
A0031011cellular_componentIno80 complex
A0031597cellular_componentcytosolic proteasome complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0033044biological_processregulation of chromosome organization
A0045739biological_processpositive regulation of DNA repair
A0045880biological_processpositive regulation of smoothened signaling pathway
A0045893biological_processpositive regulation of DNA-templated transcription
A0045995biological_processregulation of embryonic development
A0048853biological_processforebrain morphogenesis
A0051726biological_processregulation of cell cycle
A0060382biological_processregulation of DNA strand elongation
A0061136biological_processregulation of proteasomal protein catabolic process
A0070628molecular_functionproteasome binding
A1904507biological_processpositive regulation of telomere maintenance in response to DNA damage
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 329
ChainResidue
AALA80
ASER95

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 330
ChainResidue
ATRP36
ASER37
ALEU38
ALYS265
AMSE268

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 331
ChainResidue
AASP75
AGLN119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
ACYS88

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS164

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for enzyme activity => ECO:0000250
ChainResidueDetails
AASP179

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WUP7
ChainResidueDetails
ALYS47
AHIS289

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS158

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uch
ChainResidueDetails
AASP179
AHIS164
ACYS88
AGLN82

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PDB entries from 2024-05-01

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