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6F3N

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa cocrystallized with SAH in the presence of K+ and Zn2+ cations

Functional Information from GO Data
ChainGOidnamespacecontents
A0004013molecular_functionadenosylhomocysteinase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016787molecular_functionhydrolase activity
A0033353biological_processS-adenosylmethionine cycle
A0071269biological_processL-homocysteine biosynthetic process
B0004013molecular_functionadenosylhomocysteinase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
B0071269biological_processL-homocysteine biosynthetic process
C0004013molecular_functionadenosylhomocysteinase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0016787molecular_functionhydrolase activity
C0033353biological_processS-adenosylmethionine cycle
C0071269biological_processL-homocysteine biosynthetic process
D0004013molecular_functionadenosylhomocysteinase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006730biological_processone-carbon metabolic process
D0016787molecular_functionhydrolase activity
D0033353biological_processS-adenosylmethionine cycle
D0071269biological_processL-homocysteine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue K A 501
ChainResidue
AGLN65
ATHR380
AHIS382
AHOH820
AHOH859
CHOH799

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 502
ChainResidue
AHIS323
AADN505
AHIS61
ACYS85
AASP139

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 503
ChainResidue
AARG25
AILE29
AGLU32
AHOH648
CHIS360

site_idAC4
Number of Residues32
Detailsbinding site for residue NAD A 504
ChainResidue
ATHR165
ATHR166
ATHR167
AASN199
AILE227
AGLY228
AGLY230
AASP231
AVAL232
AGLU251
AVAL252
AASP253
ACYS256
ATHR297
ATHR298
AGLY299
AASN300
AVAL303
AILE321
AGLY322
AHIS323
AASN375
AHIS382
AADN505
AHOH614
AHOH780
AHOH790
AHOH804
AHOH846
AHOH850
BLYS463
BTYR467

site_idAC5
Number of Residues17
Detailsbinding site for residue ADN A 505
ChainResidue
AHIS61
ATHR63
AGLN65
ATHR66
AASP139
AGLU164
ATHR165
ALYS194
AASP198
AHIS323
ALEU373
ATHR380
AHIS382
AMET387
APHE391
AZN502
ANAD504

site_idAC6
Number of Residues6
Detailsbinding site for residue K B 501
ChainResidue
BGLN65
BTHR380
BHIS382
BHOH777
BHOH802
DHOH785

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN B 502
ChainResidue
BHIS61
BCYS85
BASP139
BHIS323
BADN505

site_idAC8
Number of Residues6
Detailsbinding site for residue PO4 B 503
ChainResidue
BARG25
BILE29
BGLU32
BHOH716
BHOH790
DHIS360

site_idAC9
Number of Residues33
Detailsbinding site for residue NAD B 504
ChainResidue
BGLY299
BASN300
BVAL303
BILE321
BGLY322
BHIS323
BLEU373
BASN375
BHIS382
BADN505
BHOH708
BHOH753
BHOH801
BHOH821
BHOH827
BHOH875
ALYS463
ATYR467
BTHR165
BTHR166
BTHR167
BASN199
BILE227
BGLY228
BGLY230
BASP231
BVAL232
BGLU251
BVAL252
BASP253
BCYS256
BTHR297
BTHR298

site_idAD1
Number of Residues16
Detailsbinding site for residue ADN B 505
ChainResidue
BHIS61
BTHR63
BGLN65
BTHR66
BASP139
BGLU164
BTHR165
BLYS194
BASP198
BHIS323
BLEU373
BTHR380
BHIS382
BMET387
BZN502
BNAD504

site_idAD2
Number of Residues5
Detailsbinding site for residue K C 501
ChainResidue
CGLN65
CTHR380
CHIS382
CHOH734
CHOH784

site_idAD3
Number of Residues5
Detailsbinding site for residue ZN C 502
ChainResidue
CHIS61
CCYS85
CASP139
CHIS323
CADN505

site_idAD4
Number of Residues5
Detailsbinding site for residue PO4 C 503
ChainResidue
AHIS360
CARG25
CILE29
CGLU32
CHOH673

site_idAD5
Number of Residues32
Detailsbinding site for residue NAD C 504
ChainResidue
CTHR165
CTHR166
CTHR167
CASN199
CILE227
CGLY228
CGLY230
CASP231
CVAL232
CGLU251
CVAL252
CASP253
CCYS256
CTHR297
CTHR298
CGLY299
CASN300
CVAL303
CILE321
CGLY322
CHIS323
CLEU373
CASN375
CHIS382
CADN505
CHOH723
CHOH754
CHOH773
CHOH787
CHOH792
DLYS463
DTYR467

site_idAD6
Number of Residues17
Detailsbinding site for residue ADN C 505
ChainResidue
CHIS61
CTHR63
CGLN65
CTHR66
CASP139
CGLU164
CTHR165
CLYS194
CASP198
CHIS323
CLEU373
CTHR380
CHIS382
CMET387
CPHE391
CZN502
CNAD504

site_idAD7
Number of Residues6
Detailsbinding site for residue K D 501
ChainResidue
BHOH847
DGLN65
DTHR380
DHIS382
DHOH752
DHOH835

site_idAD8
Number of Residues5
Detailsbinding site for residue ZN D 502
ChainResidue
DHIS61
DCYS85
DASP139
DHIS323
DADN506

site_idAD9
Number of Residues6
Detailsbinding site for residue PO4 D 503
ChainResidue
BHIS360
DARG25
DILE29
DGLU32
DHOH617
DHOH828

site_idAE1
Number of Residues7
Detailsbinding site for residue GOL D 504
ChainResidue
BGLU121
BGLN122
BGLY128
DTHR11
DTYR13
DHOH760
DHOH893

site_idAE2
Number of Residues31
Detailsbinding site for residue NAD D 505
ChainResidue
CLYS463
CTYR467
DTHR165
DTHR166
DTHR167
DASN199
DILE227
DGLY228
DGLY230
DASP231
DVAL232
DGLU251
DVAL252
DASP253
DCYS256
DTHR297
DTHR298
DGLY299
DASN300
DVAL303
DILE321
DGLY322
DHIS323
DASN375
DHIS382
DADN506
DHOH757
DHOH758
DHOH790
DHOH795
DHOH861

site_idAE3
Number of Residues16
Detailsbinding site for residue ADN D 506
ChainResidue
DHIS61
DTHR63
DGLN65
DTHR66
DASP139
DGLU164
DTHR165
DLYS194
DASP198
DHIS323
DLEU373
DTHR380
DHIS382
DMET387
DZN502
DNAD505

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDqAAAAI
ChainResidueDetails
ASER84-ILE98

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKqalViGYGdVGKGs.S
ChainResidueDetails
AGLY221-SER237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
ATHR63
AASN300
AILE321
AASN375
BTHR63
BASP139
BGLU164
BTHR165
BLYS194
BASP198
BASN199
AASP139
BGLY228
BGLU251
BASN300
BILE321
BASN375
CTHR63
CASP139
CGLU164
CTHR165
CLYS194
AGLU164
CASP198
CASN199
CGLY228
CGLU251
CASN300
CILE321
CASN375
DTHR63
DASP139
DGLU164
ATHR165
DTHR165
DLYS194
DASP198
DASN199
DGLY228
DGLU251
DASN300
DILE321
DASN375
ALYS194
AASP198
AASN199
AGLY228
AGLU251

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PDB entries from 2025-06-18

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