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2BIX

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0010436molecular_functioncarotenoid dioxygenase activity
A0016121biological_processcarotene catabolic process
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0102162molecular_functionall-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
B0010436molecular_functioncarotenoid dioxygenase activity
B0016121biological_processcarotene catabolic process
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0102162molecular_functionall-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE C8E A1491
ChainResidue
APHE69
APHE113
AHIS238
APHE303
AHIS304
ALEU483

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE C8E B1491
ChainResidue
BHIS304
BLEU483
BPHE69
BGLU150
BHIS238

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1492
ChainResidue
ASER324
AASP340
AASN341
ALEU342
AASP343

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1493
ChainResidue
ATRP20
ATYR24
ALEU400
APHE423
AALA424
AHOH2047

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15821095
ChainResidueDetails
AHIS183
BPHE303
BHIS304
BHIS484
ASER206
AHIS238
APHE303
AHIS304
AHIS484
BHIS183
BSER206
BHIS238

225946

PDB entries from 2024-10-09

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