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2HUO

Crystal structure of mouse myo-inositol oxygenase in complex with substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0008199molecular_functionferric iron binding
A0016234cellular_componentinclusion body
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0019310biological_processinositol catabolic process
A0046872molecular_functionmetal ion binding
A0050113molecular_functioninositol oxygenase activity
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FE A 301
ChainResidue
AHIS98
AHIS123
AASP124
AASP253
AFE302
AINS303
AOH304
AHOH306

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 302
ChainResidue
AHIS194
AHIS220
AFE301
AINS303
AOH304
AASP124

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OH A 304
ChainResidue
AHIS123
AASP124
AHIS220
AASP253
AFE301
AFE302
AINS303
AHOH306

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE INS A 303
ChainResidue
AARG29
ATYR44
AASP85
ASER87
AASP88
AASP124
ALYS127
AVAL140
AGLY141
AASP142
AHIS194
AHIS220
ASER221
ATYR223
AFE301
AFE302
AOH304
AHOH306
AHOH346
AHOH358

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 305
ChainResidue
AGLY147
ACYS148
AASP166

Functional Information from PROSITE/UniProt
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. MAKSKDsfRNyTSgPL
ChainResidueDetails
AMET21-LEU36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY141
AARG29
AASP85
ALYS127

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17012379, ECO:0000269|PubMed:18364358
ChainResidueDetails
AHIS194
AHIS220
AASP253
AHIS98
AHIS123
AASP124

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QXN4
ChainResidueDetails
ASER33

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PDB entries from 2024-06-12

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