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5YBP

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with preaustinoid A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0016114biological_processterpenoid biosynthetic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0140874biological_processparaherquonin biosynthetic process
B0016114biological_processterpenoid biosynthetic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0140874biological_processparaherquonin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE A 301
ChainResidue
AHIS130
AASP132
AHIS214
AAKG302
AHOH403

site_idAC2
Number of Residues11
Detailsbinding site for residue AKG A 302
ChainResidue
ATHR167
AHIS214
AALA216
AARG226
AFE301
AHOH403
AHOH425
AGLN127
AHIS130
AASP132
APHE154

site_idAC3
Number of Residues5
Detailsbinding site for residue FE B 301
ChainResidue
BHIS130
BASP132
BHIS214
BAKG302
BHOH412

site_idAC4
Number of Residues12
Detailsbinding site for residue AKG B 302
ChainResidue
BARG72
BGLN127
BHIS130
BPHE154
BTHR167
BHIS214
BALA216
BARG226
BFE301
B8SX303
BHOH410
BHOH412

site_idAC5
Number of Residues16
Detailsbinding site for residue 8SX B 303
ChainResidue
AASP276
AMET277
AVAL278
BSER66
BASN67
BARG72
BMET116
BGLN127
BARG128
BHIS130
BASP132
BLEU150
BASN152
BSER232
BMET241
BAKG302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29317628
ChainResidueDetails
AHIS130
AASP132
AHIS214
BHIS130
BASP132
BHIS214

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for reaction specificity => ECO:0000269|PubMed:29317628
ChainResidueDetails
ALEU150
ASER232
BLEU150
BSER232

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PDB entries from 2024-11-06

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