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1X9H

Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0004476molecular_functionmannose-6-phosphate isomerase activity
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016853molecular_functionisomerase activity
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0003824molecular_functioncatalytic activity
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0004476molecular_functionmannose-6-phosphate isomerase activity
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic 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 501
ChainResidue
BARG104
BARG105

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG299
AARG300

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG104
AARG105

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AHOH846
BARG79
AGLN179
AARG181
AARG284

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
BGLN179
BARG181
BARG284
BHOH780
BHOH878
BHOH894

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE F6R B 700
ChainResidue
AHIS219
BMET45
BGLY46
BGLY47
BSER48
BSER87
BTYR88
BSER89
BTHR92
BPRO134
BARG135
BGLU203
BLYS298
BHOH723
BHOH887
BHOH888

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE F6R A 701
ChainResidue
AMET45
AGLY46
AGLY47
ASER48
ASER87
ATYR88
ASER89
ATHR92
APRO134
AARG135
AGLU203
ALYS298
AHOH723
AHOH760
BHIS219

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AASP53
ALYS72
AARG191
ATYR195
AHOH739
AHOH757
AHOH784
AHOH909

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
ATHR233
AGLN242
AHOH893
AHOH898

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
ASER89
AASN91
ATHR92
AILE93
ALYS298
AHOH720
AHOH751
AHOH814
BARG117

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 605
ChainResidue
BVAL27
BGLU28
BGLU30
BLYS103
BARG104
BARG106

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_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

218853

数据于2024-04-24公开中

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