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6A34

Crystal structure of 5-methylthioribose 1-phosphate isomerase from Pyrococcus horikoshii OT3 - Form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0009086biological_processmethionine biosynthetic process
A0016853molecular_functionisomerase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0044237biological_processcellular metabolic process
A0044249biological_processcellular biosynthetic process
A0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
B0009086biological_processmethionine biosynthetic process
B0016853molecular_functionisomerase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0044237biological_processcellular metabolic process
B0044249biological_processcellular biosynthetic process
B0046523molecular_functionS-methyl-5-thioribose-1-phosphate isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue HEZ A 401
ChainResidue
ATHR332
ATRP342
ATRP342
AHOH560

site_idAC2
Number of Residues2
Detailsbinding site for residue HEZ B 401
ChainResidue
AASN162
BTYR319

site_idAC3
Number of Residues4
Detailsbinding site for residue HEZ B 402
ChainResidue
BPHE238
ATYR319
BASN162
BLYS194

site_idAC4
Number of Residues4
Detailsbinding site for residue HEZ B 403
ChainResidue
BVAL157
BTHR332
BTRP342
BPRO343

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01678
ChainResidueDetails
AASP247
BASP247

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01678
ChainResidueDetails
AARG57
AARG100
AGLN206
AASN257
BARG57
BARG100
BGLN206
BASN257

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01678
ChainResidueDetails
ACYS167
BCYS167

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PDB entries from 2024-07-24

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