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2PUP

Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0009086biological_processmethionine biosynthetic process
A0016301molecular_functionkinase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0046522molecular_functionS-methyl-5-thioribose kinase activity
B0005524molecular_functionATP binding
B0009086biological_processmethionine biosynthetic process
B0016301molecular_functionkinase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0046522molecular_functionS-methyl-5-thioribose kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 400
ChainResidue
AASP250
AGLU252
AADP999

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP250
AADP999

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 400
ChainResidue
BASP250
BGLU252
BPO4998
BADP999

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP250
BPO4998
BADP999

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 998
ChainResidue
BASP233
BHIS235
BASP250
BMG400
BMG401
BADP999

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CPS B 777
ChainResidue
ALYS377
AGLU380
AASP386
AGLU389
ALEU393
BLYS377
BGLU380
BLEU394
BHOH1012
BHOH1119

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 999
ChainResidue
AASN44
AILE59
ALYS61
AGLU115
AASP116
ALEU117
ASER118
APHE240
AILE249
AASP250
AGLU252
AMG400
AMG401

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 999
ChainResidue
BASN44
BILE59
BLYS61
BMET114
BGLU115
BASP116
BLEU117
BSER118
BPHE240
BASP250
BGLU252
BMG400
BMG401
BPO4998

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17372354, ECO:0000269|PubMed:17522047
ChainResidueDetails
AASN44
ALYS61
AGLU115
AASP250
BASN44
BLYS61
BGLU115
BASP250

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17522047
ChainResidueDetails
AASP233
AARG340
BASP233
BARG340

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
AASP233

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
BASP233

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PDB entries from 2024-07-24

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