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1DKN

CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 5.0 WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0003993molecular_functionacid phosphatase activity
A0008252molecular_functionnucleotidase activity
A0008707molecular_function4-phytase activity
A0016036biological_processcellular response to phosphate starvation
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0050308molecular_functionsugar-phosphatase activity
A0052745molecular_functioninositol phosphate phosphatase activity
A0071454biological_processcellular response to anoxia
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 500
ChainResidue
AHIS113
AASP154
AHIS158
ATYR289
AHOH708

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HG A 501
ChainResidue
AASP325
AHOH690
AHOH691
AARG16
AGLU219
AHIS250
AASP304

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 502
ChainResidue
AHIS282
AGLN285
AGLN287
ALEU293
AHOH715

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 503
ChainResidue
AALA278
APRO294
ATHR295
AHG504

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 504
ChainResidue
ASER10
AVAL11
ASER296
ALEU298
AHG503

Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LesVviVsRHGvRaP
ChainResidueDetails
ALEU8-PRO22

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. VlFIaGHDTNLanLggA
ChainResidueDetails
AVAL297-ALA313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:1429631
ChainResidueDetails
AHIS17

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:8407904
ChainResidueDetails
AASP304

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ
ChainResidueDetails
AARG92
AHIS303
AARG16
AARG20

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ
ChainResidueDetails
AARG267

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PDB entries from 2024-06-12

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