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3O1X

High resolution crystal structure of histidine triad nucleotide-binding protein 1 (Hint1) C84A mutant from rabbit complexed with adenosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006355biological_processregulation of DNA-templated transcription
A0006508biological_processproteolysis
A0006790biological_processsulfur compound metabolic process
A0006915biological_processapoptotic process
A0008234molecular_functioncysteine-type peptidase activity
A0009154biological_processpurine ribonucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016926biological_processprotein desumoylation
A0016929molecular_functiondeSUMOylase activity
A0043530molecular_functionadenosine 5'-monophosphoramidase activity
A0047627molecular_functionadenylylsulfatase activity
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADN A 1450
ChainResidue
APHE19
AHIS114
AHOH136
AHOH156
AHOH179
AHOH220
AHOH229
AHOH235
AHOH251
AHOH314
ALYS25
AGLU34
AHIS42
AASP43
AILE44
ASER45
ALEU53
AHIS112

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 127
ChainResidue
ALYS83
AASP87
AHOH166
AHOH193
AHOH307

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. NegsdGgQsVyHVHLHVLG
ChainResidueDetails
AASN99-GLY117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000250|UniProtKB:P49773
ChainResidueDetails
AHIS112

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P49773
ChainResidueDetails
AASN99
AGLY105
AHIS112
AASP43

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P62958
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49773
ChainResidueDetails
ALYS30
ALYS21

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70349
ChainResidueDetails
ASER45
ASER72

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PDB entries from 2024-06-12

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