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5TOW

Crystal structure of the inactive form of S-adenosyl-L-homocysteine hydrolase from Thermotoga maritima in ternary complex with NADH and Adenosine

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
B0004013molecular_functionadenosylhomocysteinase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ADN A 501
ChainResidue
AGLY203
AHOH718
AHOH729
ATHR225
AGLU226
AASP228
ALYS231
ASER259
AASN261
AGLN396
AHOH693

site_idAC2
Number of Residues4
Detailsbinding site for residue MPD A 502
ChainResidue
AVAL230
AASP374
AHOH740
AHOH741

site_idAC3
Number of Residues30
Detailsbinding site for residue NAI B 501
ChainResidue
BTHR140
BTHR141
BTHR142
BGLY203
BGLY205
BTRP206
BCYS207
BTHR225
BGLU226
BVAL227
BASP228
BLYS231
BALA258
BSER259
BGLY260
BASN261
BALA282
BGLY283
BHIS284
BLEU327
BASN329
BGLN396
BHOH620
BHOH633
BHOH660
BHOH697
BHOH731
BHOH733
BHOH785
BHOH790

site_idAC4
Number of Residues5
Detailsbinding site for residue CL B 502
ChainResidue
AGLN180
AARG214
BARG175
BTYR176
BARG214

site_idAC5
Number of Residues1
Detailsbinding site for residue CL B 503
ChainResidue
AHOH694

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. GSNpLSTQDdVAEAL
ChainResidueDetails
AGLY64-LEU78

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKnvvVaGYGwCGRGi.A
ChainResidueDetails
AGLY196-ALA212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
AGLY203
AGLU226
AASN261
AALA282
AASN329
BASP114
BGLU139
BTHR140
BLYS169
BASP173
BASN174
BGLY203
BGLU226
BASN261
BALA282
BASN329
AASP114
AGLU139
ATHR140
ALYS169
AASP173
AASN174

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PDB entries from 2024-06-12

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