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6EXH

Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Fe(II)/succinate/(4R)-4-hydroxy-L-lysine

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
ASIN403

site_idAC2
Number of Residues10
Detailsbinding site for residue LYO A 402
ChainResidue
AASP230
AARG338
ASIN403
AHOH622
AHOH639
ATRP112
AARG145
AGLY166
ASER167
AGLU178

site_idAC3
Number of Residues14
Detailsbinding site for residue SIN A 403
ChainResidue
ALEU173
AHIS176
AGLU178
APHE191
ATYR193
AHIS312
AARG314
AARG334
AMET336
AARG338
AFE401
ALYO402
AHOH513
AHOH517

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 404
ChainResidue
ATHR354
AASP355

site_idAC5
Number of Residues4
Detailsbinding site for residue FE B 401
ChainResidue
BHIS176
BGLU178
BHIS312
BSIN403

site_idAC6
Number of Residues12
Detailsbinding site for residue LYO B 402
ChainResidue
BGLN144
BGLN164
BGLY166
BHIS176
BGLU178
BASP260
BARG338
BSIN403
BHOH529
BHOH537
BHOH543
BHOH562

site_idAC7
Number of Residues12
Detailsbinding site for residue SIN B 403
ChainResidue
BVAL154
BGLY166
BLEU173
BHIS176
BGLU178
BHIS312
BARG314
BARG334
BMET336
BARG338
BFE401
BLYO402

site_idAC8
Number of Residues4
Detailsbinding site for residue FE C 401
ChainResidue
CHIS176
CGLU178
CHIS312
CHOH565

site_idAC9
Number of Residues10
Detailsbinding site for residue LYO C 402
ChainResidue
CGLN144
CGLN164
CTHR165
CGLY166
CHIS176
CGLU178
CASN232
CGLU263
CARG338
CHOH528

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL C 403
ChainResidue
CGLN102
CASP103
CGLY106
CPRO107
CARG195
CGLU332

site_idAD2
Number of Residues5
Detailsbinding site for residue FE D 401
ChainResidue
DHIS176
DGLU178
DHIS312
DSIN402
DHOH572

site_idAD3
Number of Residues13
Detailsbinding site for residue SIN D 402
ChainResidue
DHIS176
DGLU178
DPHE191
DTYR193
DHIS312
DGLY313
DARG334
DMET336
DARG338
DFE401
DLYO404
DHOH572
DHOH590

site_idAD4
Number of Residues2
Detailsbinding site for residue GOL D 403
ChainResidue
DALA48
DHIS64

site_idAD5
Number of Residues12
Detailsbinding site for residue LYO D 404
ChainResidue
DGLN164
DTHR165
DGLY166
DHIS176
DGLU178
DASP230
DASN232
DASP260
DARG338
DSIN402
DHOH530
DGLN144

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

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PDB entries from 2024-10-16

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