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6EUR

Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Fe(II)/alpha-ketoglutarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0055114biological_processobsolete oxidation-reduction process
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0055114biological_processobsolete oxidation-reduction process
C0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0055114biological_processobsolete oxidation-reduction process
D0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE A 401
ChainResidue
AHIS176
AGLU178
AHIS312
AAKG402

site_idAC2
Number of Residues13
Detailsbinding site for residue AKG A 402
ChainResidue
AHIS312
AARG314
AARG334
AMET336
AARG338
AFE401
AHOH543
AHOH555
ALEU173
AHIS176
AGLU178
APHE191
ATYR193

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
AARG353
ATHR354
AASP355
AMET361
AHOH589

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AGLU53
AGLN140
AASP356
ATYR358

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 405
ChainResidue
AGLU53
AGLY148
AGLY149
AHOH644
DLYS159

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 406
ChainResidue
AALA245
ASER246
ATYR249
AARG258

site_idAC7
Number of Residues5
Detailsbinding site for residue FE B 401
ChainResidue
BHIS176
BGLU178
BHIS312
BAKG402
BHOH620

site_idAC8
Number of Residues12
Detailsbinding site for residue AKG B 402
ChainResidue
BVAL154
BHIS176
BGLU178
BPHE191
BTYR193
BHIS312
BGLY313
BARG334
BMET336
BARG338
BFE401
BHOH590

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL B 403
ChainResidue
BGLN33
DLEU44
DLEU45

site_idAD1
Number of Residues5
Detailsbinding site for residue FE C 401
ChainResidue
CHIS176
CGLU178
CHIS312
CAKG402
CHOH595

site_idAD2
Number of Residues14
Detailsbinding site for residue AKG C 402
ChainResidue
CVAL154
CLEU173
CHIS176
CGLU178
CPHE191
CTYR193
CHIS312
CGLY313
CARG314
CARG334
CARG338
CFE401
CHOH528
CHOH556

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL C 403
ChainResidue
CGLU53
CGLN140
CASP356
CTYR358
CHOH535

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL C 404
ChainResidue
CGLN102
CASP103
CGLY106
CPRO107
CARG195
CGLU332

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL C 405
ChainResidue
CTHR352
CTHR354
CMET361
CILE368

site_idAD6
Number of Residues4
Detailsbinding site for residue FE D 401
ChainResidue
DHIS176
DGLU178
DHIS312
DAKG402

site_idAD7
Number of Residues11
Detailsbinding site for residue AKG D 402
ChainResidue
DARG314
DARG334
DMET336
DARG338
DFE401
DLEU173
DHIS176
DGLU178
DPHE191
DTYR193
DHIS312

site_idAD8
Number of Residues6
Detailsbinding site for residue GOL D 403
ChainResidue
DASP172
DPHE174
DVAL175
DILE291
DHOH550
DHOH561

site_idAD9
Number of Residues3
Detailsbinding site for residue GOL D 404
ChainResidue
DTRP112
DARG145
DSER167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Z4Z5
ChainResidueDetails
AHIS176
DHIS176
DGLU178
DHIS312
AGLU178
AHIS312
BHIS176
BGLU178
BHIS312
CHIS176
CGLU178
CHIS312

226707

PDB entries from 2024-10-30

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