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5YBO

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA 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
AHOH408

site_idAC2
Number of Residues11
Detailsbinding site for residue AKG A 302
ChainResidue
ATHR167
AHIS214
AALA216
AARG226
AFE301
AHOH408
AHOH429
AGLN127
AHIS130
AASP132
APHE154

site_idAC3
Number of Residues5
Detailsbinding site for residue FE B 301
ChainResidue
BHIS130
BASP132
BHIS214
BAKG302
BHOH421

site_idAC4
Number of Residues13
Detailsbinding site for residue AKG B 302
ChainResidue
BARG72
BILE118
BGLN127
BHIS130
BASP132
BPHE154
BTHR167
BHIS214
BALA216
BARG226
BFE301
B8SX303
BHOH421

site_idAC5
Number of Residues17
Detailsbinding site for residue 8SX B 303
ChainResidue
AASP276
AMET277
AVAL278
BSER66
BASN67
BARG72
BASN113
BMET116
BGLN127
BARG128
BHIS130
BASP132
BVAL150
BASN152
BALA232
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
AVAL150
AALA232
BVAL150
BALA232

219869

PDB entries from 2024-05-15

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