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

8COD

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Mus musculus in complex with inosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0002439biological_processchronic inflammatory response to antigenic stimulus
A0004013molecular_functionadenosylhomocysteinase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0007584biological_processresponse to nutrient
A0016787molecular_functionhydrolase activity
A0019510biological_processS-adenosylhomocysteine catabolic process
A0030554molecular_functionadenyl nucleotide binding
A0033353biological_processS-adenosylmethionine cycle
A0042470cellular_componentmelanosome
A0042745biological_processcircadian sleep/wake cycle
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
B0002439biological_processchronic inflammatory response to antigenic stimulus
B0004013molecular_functionadenosylhomocysteinase activity
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0007584biological_processresponse to nutrient
B0016787molecular_functionhydrolase activity
B0019510biological_processS-adenosylhomocysteine catabolic process
B0030554molecular_functionadenyl nucleotide binding
B0033353biological_processS-adenosylmethionine cycle
B0042470cellular_componentmelanosome
B0042745biological_processcircadian sleep/wake cycle
B0042802molecular_functionidentical protein binding
B0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI
ChainResidueDetails
ASER78-ILE92

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A
ChainResidueDetails
AGLY213-ALA229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10760
ChainResidueDetails
ATHR57
AASP131
AGLU156
ALYS186
AASP190
BTHR57
BASP131
BGLU156
BLYS186
BASP190

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ASER183
BSER183

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ALYS186
BLYS186

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATYR193
BTYR193

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon