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3RHN

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP

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
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009154biological_processpurine ribonucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016926biological_processprotein desumoylation
A0016929molecular_functiondeSUMOylase activity
A0043530molecular_functionadenosine 5'-monophosphoramidase activity
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 5GP A 201
ChainResidue
AASN99
AGLY105
AGLN106
ASER107
AVAL108
AHIS112
AHIS114
AHOH219
AHOH235
APHE19
APHE41
AHIS42
AASP43
AILE44
ALEU53

site_idHIT
Number of Residues3
DetailsTHE HISTIDINE TRIAD FORMS PART OF THE ALPHA PHOSPHATE-BINDING LOOP IN THE HIT PROTEIN SUPERFAMILY OF NUCLEOTIDE-BINDING PROTEINS.
ChainResidue
AHIS110
AHIS112
AHIS114

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 Residues108
DetailsDomain: {"description":"HIT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00464","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"Histidine triad motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"UniProtKB","id":"P49773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P49773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P49773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P70349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 5fit
ChainResidueDetails
AHIS112
AASN99
AHIS110

238895

PDB entries from 2025-07-16

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