Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5ZDQ

Crystal structure of cyanide-insensitive alternative oxidase from Trypanosoma brucei with COLLETOCHLORIN B

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0008199molecular_functionferric iron binding
A0009916molecular_functionalternative oxidase activity
A0010230biological_processalternative respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0043229cellular_componentintracellular organelle
A0046872molecular_functionmetal ion binding
A0070469cellular_componentrespirasome
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0008199molecular_functionferric iron binding
B0009916molecular_functionalternative oxidase activity
B0010230biological_processalternative respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0043229cellular_componentintracellular organelle
B0046872molecular_functionmetal ion binding
B0070469cellular_componentrespirasome
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0008199molecular_functionferric iron binding
C0009916molecular_functionalternative oxidase activity
C0010230biological_processalternative respiration
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0043229cellular_componentintracellular organelle
C0046872molecular_functionmetal ion binding
C0070469cellular_componentrespirasome
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0008199molecular_functionferric iron binding
D0009916molecular_functionalternative oxidase activity
D0010230biological_processalternative respiration
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0043229cellular_componentintracellular organelle
D0046872molecular_functionmetal ion binding
D0070469cellular_componentrespirasome
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue FE A 501
ChainResidue
AGLU123
AGLU162
AHIS165
AGLU266
AFE502
AOH503

site_idAC2
Number of Residues6
Detailsbinding site for residue FE A 502
ChainResidue
AFE501
AOH503
AHOH633
AGLU162
AGLU213
AGLU266

site_idAC3
Number of Residues8
Detailsbinding site for residue OH A 503
ChainResidue
AGLU123
AALA126
AGLU162
AGLU213
AGLU266
AFE501
AFE502
ARNB504

site_idAC4
Number of Residues11
Detailsbinding site for residue RNB A 504
ChainResidue
AVAL92
AARG96
AARG118
ALEU122
AGLU123
ALEU212
AGLU215
AALA216
ATHR219
AOH503
AHOH633

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 505
ChainResidue
AARG173
APRO175
AGLY176
ALEU179
AHOH627

site_idAC6
Number of Residues6
Detailsbinding site for residue FE B 501
ChainResidue
BGLU123
BGLU162
BHIS165
BGLU266
BFE502
BOH503

site_idAC7
Number of Residues6
Detailsbinding site for residue FE B 502
ChainResidue
BGLU162
BGLU213
BGLU266
BFE501
BOH503
BHOH614

site_idAC8
Number of Residues7
Detailsbinding site for residue OH B 503
ChainResidue
BGLU123
BALA126
BGLU162
BGLU266
BFE501
BFE502
BRNB504

site_idAC9
Number of Residues7
Detailsbinding site for residue RNB B 504
ChainResidue
BARG96
BARG118
BLEU122
BLEU212
BGLU215
BTHR219
BOH503

site_idAD1
Number of Residues6
Detailsbinding site for residue FE C 501
ChainResidue
CGLU123
CGLU162
CHIS165
CGLU266
CFE502
COH503

site_idAD2
Number of Residues6
Detailsbinding site for residue FE C 502
ChainResidue
CGLU162
CGLU213
CGLU266
CFE501
COH503
CHOH612

site_idAD3
Number of Residues7
Detailsbinding site for residue OH C 503
ChainResidue
CGLU123
CALA126
CGLU162
CGLU266
CFE501
CFE502
CRNB504

site_idAD4
Number of Residues12
Detailsbinding site for residue RNB C 504
ChainResidue
CPHE99
CARG118
CCYS119
CLEU122
CGLU123
CLEU212
CGLU215
CALA216
CTHR219
CTYR220
COH503
CHOH612

site_idAD5
Number of Residues6
Detailsbinding site for residue FE D 501
ChainResidue
DGLU123
DGLU162
DHIS165
DGLU266
DFE502
DOH503

site_idAD6
Number of Residues6
Detailsbinding site for residue FE D 502
ChainResidue
DGLU162
DGLU213
DGLU266
DFE501
DOH503
DHOH630

site_idAD7
Number of Residues7
Detailsbinding site for residue OH D 503
ChainResidue
DGLU123
DALA126
DGLU162
DGLU266
DFE501
DFE502
DRNB504

site_idAD8
Number of Residues11
Detailsbinding site for residue RNB D 504
ChainResidue
DVAL92
DARG96
DARG118
DLEU122
DGLU123
DLEU212
DGLU215
DALA216
DTHR219
DOH503
DHOH630

site_idAD9
Number of Residues5
Detailsbinding site for residue SO4 D 505
ChainResidue
DSER117
DARG173
DPRO175
DGLY176
DLEU179

site_idAE1
Number of Residues2
Detailsbinding site for residue GOL D 506
ChainResidue
DASN286
DHOH642

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL115-MET135
AVAL181-SER201
BVAL115-MET135
BVAL181-SER201
CVAL115-MET135
CVAL181-SER201
DVAL115-MET135
DVAL181-SER201

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23487766, ECO:0007744|PDB:3W54
ChainResidueDetails
AGLU123
BGLU213
BGLU266
BHIS269
CGLU123
CGLU162
CHIS165
CGLU213
CGLU266
CHIS269
DGLU123
AGLU162
DGLU162
DHIS165
DGLU213
DGLU266
DHIS269
AHIS165
AGLU213
AGLU266
AHIS269
BGLU123
BGLU162
BHIS165

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon