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1TZB

Crystal structure of native phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0004476molecular_functionmannose-6-phosphate isomerase activity
A0005975biological_processcarbohydrate metabolic process
A0016853molecular_functionisomerase activity
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0004476molecular_functionmannose-6-phosphate isomerase activity
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 701
ChainResidue
BARG104
BARG105

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AARG299
AARG300

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
ATYR101
AARG104
AARG105

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 705
ChainResidue
BTYR88
BSER89
BTHR92
BPRO134
BHOH733
BHOH943
BHOH946
BSER48
BSER87

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 706
ChainResidue
AGLN179
AARG181
AARG284
AHOH957
AHOH1036
AHOH1038
BARG79

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 707
ChainResidue
BPRO160
BGLU161
BGLY162
BLYS264

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 708
ChainResidue
BGLN179
BARG181
BARG284
BHOH792
BHOH921
BHOH995
BHOH996

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 709
ChainResidue
ASER48
ASER87
ATYR88
ASER89
ATHR92
APRO134
AHOH822
AHOH862
AHOH1062

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
AASP53
AALA70
ALYS72
AARG191
ATYR195
AHOH837
AHOH883
AHOH965
AHOH1099
AHOH1133

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 802
ChainResidue
ATHR233
AGLN242
AHOH1054
AHOH1070

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU203
ALYS298
BGLU203
BLYS298

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AHIS219
BHIS219

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ASER48
ASER87
ATHR92
BSER48
BSER87
BTHR92

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1x9h
ChainResidueDetails
AARG135
ALYS298
AHIS219
AGLU203

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1x9h
ChainResidueDetails
BARG135
BLYS298
BHIS219
BGLU203

site_idMCSA1
Number of Residues4
DetailsM-CSA 736
ChainResidueDetails
AARG135electrostatic stabiliser
AGLU203proton acceptor, proton donor
AHIS219proton acceptor, proton donor
ALYS298proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 736
ChainResidueDetails
BARG135electrostatic stabiliser
BGLU203proton acceptor, proton donor
BHIS219proton acceptor, proton donor
BLYS298proton acceptor, proton donor

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PDB entries from 2024-07-24

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