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5AXA

Crystal structure of mouse SAHH complexed with adenosine

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
C0002439biological_processchronic inflammatory response to antigenic stimulus
C0004013molecular_functionadenosylhomocysteinase activity
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0007584biological_processresponse to nutrient
C0016787molecular_functionhydrolase activity
C0019510biological_processS-adenosylhomocysteine catabolic process
C0030554molecular_functionadenyl nucleotide binding
C0033353biological_processS-adenosylmethionine cycle
C0042470cellular_componentmelanosome
C0042745biological_processcircadian sleep/wake cycle
C0042802molecular_functionidentical protein binding
C0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues33
Detailsbinding site for residue NAD A 501
ChainResidue
ATHR157
AILE244
AASP245
AASN248
ATHR275
ATHR276
AGLY277
ACYS278
AILE281
AILE299
AGLY300
ATHR158
AHIS301
ALEU344
AASN346
AHIS353
AGLN413
ALYS426
ATYR430
AADN502
AHOH722
AHOH737
ATHR159
AHOH853
AHOH854
AHOH888
AHOH898
AASN191
AGLY222
AASP223
AVAL224
ATHR242
AGLU243

site_idAC2
Number of Residues15
Detailsbinding site for residue ADN A 502
ChainResidue
AHIS55
ATHR57
AGLU59
ATHR60
AASP131
AGLU156
ATHR157
ALYS186
AASP190
AHIS301
AMET351
AHIS353
AMET358
APHE362
ANAD501

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
AGLU59
AHOH774
AHOH801
AHOH1059
CASP208
CHOH655

site_idAC4
Number of Residues33
Detailsbinding site for residue NAD C 501
ChainResidue
CTHR157
CTHR158
CTHR159
CASN191
CGLY222
CASP223
CVAL224
CTHR242
CGLU243
CILE244
CASP245
CASN248
CTHR275
CTHR276
CGLY277
CCYS278
CILE281
CILE299
CGLY300
CHIS301
CLEU344
CASN346
CHIS353
CGLN413
CLYS426
CTYR430
CADN502
CHOH673
CHOH773
CHOH877
CHOH890
CHOH895
CHOH906

site_idAC5
Number of Residues15
Detailsbinding site for residue ADN C 502
ChainResidue
CMET358
CPHE362
CNAD501
CHIS55
CTHR57
CGLU59
CTHR60
CASP131
CGLU156
CTHR157
CLYS186
CASP190
CHIS301
CMET351
CHIS353

site_idAC6
Number of Residues6
Detailsbinding site for residue NA C 503
ChainResidue
AASP208
AHOH676
CGLU59
CHOH816
CHOH819
CHOH1071

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
CASP190
AASP131
AGLU156
ALYS186
AASP190
CTHR57
CASP131
CGLU156
CLYS186

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ASER2
CSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ASER183
CSER183

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526
ChainResidueDetails
ALYS186
CLYS186

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATYR193
CTYR193

223166

PDB entries from 2024-07-31

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