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2BIW

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, native enzyme

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
C0010436molecular_functioncarotenoid dioxygenase activity
C0016121biological_processcarotene catabolic process
C0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0102162molecular_functionall-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
D0010436molecular_functioncarotenoid dioxygenase activity
D0016121biological_processcarotene catabolic process
D0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0102162molecular_functionall-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A1492
ChainResidue
AHIS183
AHIS238
AHIS304
AHIS484
AHOH2089

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B1492
ChainResidue
BHOH2079
BHIS183
BHIS238
BHIS304
BHIS484

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C1492
ChainResidue
CHIS183
CHIS238
CHIS304
CHIS484
CHOH2121

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D1492
ChainResidue
DHIS183
DHIS238
DHIS304
DHIS484
DHOH2052

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 3ON A1491
ChainResidue
APHE69
ALEU130
ATHR136
ATRP149
AGLU150
AGLY151
ASER206
APHE236
AHIS238
APHE303
ATYR322
AGLU370
APHE371
ALEU400
AHOH2008
AHOH2035
AHOH2064
AHOH2084

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3ON B1491
ChainResidue
BPHE69
BLEU130
BTHR136
BTRP149
BSER206
BHIS238
BPHE303
BTYR322
BLEU400
BHOH2022
BHOH2042
BHOH2075

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3ON C1491
ChainResidue
CPHE69
CPHE113
CLEU130
CTHR136
CTRP149
CGLU150
CGLY151
CSER206
CPHE236
CHIS238
CPHE303
CTYR322
CGLU370
CPHE371
CHOH2042

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3ON D1491
ChainResidue
DPHE69
DVAL112
DTHR136
DTRP149
DGLU150
DGLY151
DPHE236
DHIS238
DGLY269
DPHE303
DGLU370
DHOH2005
DHOH2020
DHOH2047
DHOH2065

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:15821095
ChainResidueDetails
AHIS183
CHIS304
CHIS484
DHIS183
DSER206
DHIS238
DPHE303
DHIS304
DHIS484
ASER206
AHIS238
APHE303
AHIS304
AHIS484
BHIS183
BSER206
BHIS238
BPHE303
BHIS304
BHIS484
CHIS183
CSER206
CHIS238
CPHE303

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PDB entries from 2024-05-01

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