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1IHP

STRUCTURE OF PHOSPHOMONOESTERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0005576cellular_componentextracellular region
A0016158molecular_function3-phytase activity
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 445
ChainResidue
AARG163
AARG423

Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. VtfAqvLsRHGaRyP
ChainResidueDetails
AVAL50-PRO64

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LyADfSHDNGIisIlfA
ChainResidueDetails
ALEU332-ALA348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9164457, ECO:0007744|PDB:1IHP
ChainResidueDetails
AHIS59

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q
ChainResidueDetails
AGLN27
AHIS338
AASP339
ATYR28
AARG58
AHIS59
AARG62
ATHR65
AARG142
AASP188
ALYS278

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4P, ECO:0007744|PDB:3K4Q
ChainResidueDetails
AASN82
AASN316
AASN353

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4Q
ChainResidueDetails
AASN184

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rpt
ChainResidueDetails
AARG58
AARG142
AHIS338
AASP339
AARG62
AHIS59

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PDB entries from 2024-07-10

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