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6F3P

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa in complex with 3'-deoxyadenosine and K+ cation

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
C0004013molecular_functionadenosylhomocysteinase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0016787molecular_functionhydrolase activity
C0033353biological_processS-adenosylmethionine cycle
C0071269biological_processL-homocysteine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue NAD A 501
ChainResidue
ATHR166
AVAL252
AASP253
ACYS256
ATHR297
ATHR298
AGLY299
AASN300
AVAL303
AILE321
AGLY322
ATHR167
AHIS323
AASN375
AHIS382
A3AD502
ACL504
AHOH652
AHOH731
AHOH855
CLYS463
CTYR467
AASN199
CHOH998
CHOH1026
CHOH1144
AILE227
AGLY228
AGLY230
AASP231
AVAL232
AGLU251

site_idAC2
Number of Residues14
Detailsbinding site for residue 3AD A 502
ChainResidue
AHIS61
ATHR63
AGLN65
ATHR66
AASP139
AGLU164
ALYS194
AASP198
AHIS323
ATHR380
AHIS382
AMET387
ANAD501
ACL504

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 503
ChainResidue
AGLN65
ATHR380
AHIS382
AHOH826
AHOH863
CHOH827

site_idAC4
Number of Residues7
Detailsbinding site for residue CL A 504
ChainResidue
ATHR165
ATHR166
AASN189
ALYS194
AASN199
ANAD501
A3AD502

site_idAC5
Number of Residues7
Detailsbinding site for residue PO4 A 505
ChainResidue
AARG25
AILE29
AGLU32
AHOH641
AHOH804
AHOH817
CHIS360

site_idAC6
Number of Residues32
Detailsbinding site for residue NAD C 501
ChainResidue
ALYS463
ATYR467
AHOH946
AHOH969
CTHR166
CTHR167
CASN199
CILE227
CGLY228
CGLY230
CASP231
CVAL232
CGLU251
CVAL252
CASP253
CCYS256
CTHR297
CTHR298
CGLY299
CASN300
CVAL303
CILE321
CGLY322
CHIS323
CASN375
CHIS382
C3AD502
CCL504
CHOH633
CHOH733
CHOH744
CHOH876

site_idAC7
Number of Residues16
Detailsbinding site for residue 3AD C 502
ChainResidue
CTHR63
CGLN65
CTHR66
CASP139
CGLU164
CLYS194
CASP198
CHIS323
CLEU373
CTHR380
CHIS382
CMET387
CPHE391
CNAD501
CCL504
CHIS61

site_idAC8
Number of Residues6
Detailsbinding site for residue K C 503
ChainResidue
AHOH780
CGLN65
CTHR380
CHIS382
CHOH842
CHOH890

site_idAC9
Number of Residues7
Detailsbinding site for residue CL C 504
ChainResidue
CTHR165
CTHR166
CASN189
CLYS194
CASN199
CNAD501
C3AD502

site_idAD1
Number of Residues8
Detailsbinding site for residue PO4 C 505
ChainResidue
AHIS360
CARG25
CILE29
CGLU32
CHOH640
CHOH735
CHOH914
CHOH993

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 Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
ATHR63
AASN300
AILE321
AASN375
CTHR63
CASP139
CGLU164
CTHR165
CLYS194
CASP198
CASN199
AASP139
CGLY228
CGLU251
CASN300
CILE321
CASN375
AGLU164
ATHR165
ALYS194
AASP198
AASN199
AGLY228
AGLU251

222415

PDB entries from 2024-07-10

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