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

3DP9

Crystal structure of Vibrio cholerae 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with butylthio-DADMe-Immucillin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009086biological_processmethionine biosynthetic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0008782molecular_functionadenosylhomocysteine nucleosidase activity
C0008930molecular_functionmethylthioadenosine nucleosidase activity
C0009086biological_processmethionine biosynthetic process
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016787molecular_functionhydrolase activity
C0019284biological_processL-methionine salvage from S-adenosylmethionine
C0019509biological_processL-methionine salvage from methylthioadenosine
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD C 300
ChainResidue
ATHR139
CPRO137
CTHR139

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BIG A 301
ChainResidue
AVAL153
AVAL172
AGLU173
AMET174
AGLU175
ASER197
AASP198
APHE208
AHOH305
CPHE105
AILE50
ASER76
AALA77
AGLY78
AALA151
APHE152

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BIG C 301
ChainResidue
CILE50
CSER76
CALA77
CGLY78
CALA151
CPHE152
CVAL153
CVAL172
CGLU173
CMET174
CGLU175
CSER197
CASP198
CPHE208
CHOH302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AGLU12
CGLU12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AASP198
CASP198

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AGLY78
AVAL153
AMET174
CGLY78
CVAL153
CMET174

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a69
ChainResidueDetails
APHE211
AASP198

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a69
ChainResidueDetails
CPHE211
CASP198

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon