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6RMR

Crystal structure of Escherichia coli periplasmic glucose-1-phosphatase H18D mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0006007biological_processglucose catabolic process
A0008877molecular_functionglucose-1-phosphatase activity
A0016158molecular_function3-phytase activity
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0050308molecular_functionsugar-phosphatase activity
B0006007biological_processglucose catabolic process
B0008877molecular_functionglucose-1-phosphatase activity
B0016158molecular_function3-phytase activity
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0050308molecular_functionsugar-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue 1PE A 401
ChainResidue
AGLU196
AHIS289
AASP290
ASER291
AACT407

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 402
ChainResidue
ATHR104
ACYS110
AILE112
BACT402

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT A 403
ChainResidue
ACYS79
APRO80
AASP111

site_idAC4
Number of Residues3
Detailsbinding site for residue ACT A 404
ChainResidue
AGLN93
AGLY121
AHOH518

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 405
ChainResidue
ALEU297
ATHR298
APHE302

site_idAC6
Number of Residues3
Detailsbinding site for residue ACT A 406
ChainResidue
ALEU182
AHOH503
BGLU5

site_idAC7
Number of Residues6
Detailsbinding site for residue ACT A 407
ChainResidue
AARG17
AASP18
AARG94
AHIS289
AASP290
A1PE401

site_idAC8
Number of Residues2
Detailsbinding site for residue ACT A 408
ChainResidue
ALEU9
AGLN10

site_idAC9
Number of Residues3
Detailsbinding site for residue ZN A 409
ChainResidue
AASP270
AASP383
AASN387

site_idAD1
Number of Residues2
Detailsbinding site for residue ACT B 401
ChainResidue
BTRP237
BASN311

site_idAD2
Number of Residues3
Detailsbinding site for residue ACT B 402
ChainResidue
AACT402
BTHR104
BILE112

site_idAD3
Number of Residues1
Detailsbinding site for residue ACT B 403
ChainResidue
AHIS326

site_idAD4
Number of Residues2
Detailsbinding site for residue ACT B 404
ChainResidue
BASN167
BLYS169

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT B 405
ChainResidue
AGLN306
AVAL362
BASP380
BASP383
BASN387

site_idAD6
Number of Residues4
Detailsbinding site for residue ACT B 406
ChainResidue
BASP18
BARG94
BHIS289
BASP290

site_idAD7
Number of Residues2
Detailsbinding site for residue ACT B 407
ChainResidue
BTYR88
BGLN117

site_idAD8
Number of Residues5
Detailsbinding site for residue ACT B 408
ChainResidue
BGLN48
BLEU92
BGLN93
BGLY121
BHOH518

site_idAD9
Number of Residues4
Detailsbinding site for residue ACT B 409
ChainResidue
ASER76
APRO108
BVAL44
BGLN48

site_idAE1
Number of Residues2
Detailsbinding site for residue EDO B 410
ChainResidue
BGLU196
BSER291

site_idAE2
Number of Residues1
Detailsbinding site for residue EDO B 411
ChainResidue
BGLU219

Functional Information from PROSITE/UniProt
site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. ItVLvGHDSNIasLltA
ChainResidueDetails
AILE283-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP18
BASP18

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP290
BASP290

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
BGLU196
BHIS289
AHIS289
BARG17
BARG21
AARG17
AARG21
AARG94
AGLU196
BARG94

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PDB entries from 2024-06-12

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