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3IQ5

Crystal structure of an engineered metal-free tetrameric cytochrome cb562 complex templated by Zn-coordination

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
C0005506molecular_functioniron ion binding
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
C0022900biological_processelectron transport chain
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
D0005506molecular_functioniron ion binding
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
D0022900biological_processelectron transport chain
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 150
ChainResidue
AGLU4
AHIS102
ATYR105
AHOH149
AHOH153
AMET7
AGLU8
AASN11
APHE61
APHE65
ALEU68
ACYS98
ACYS101

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 150
ChainResidue
BGLU4
BMET7
BGLU8
BASN11
BLEU14
BPRO45
BPHE61
BPHE65
BCYS98
BCYS101
BHIS102
BARG106
BHOH110
BHOH129
BHOH183

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM C 150
ChainResidue
CGLU4
CMET7
CGLU8
CASN11
CLEU14
CMET33
CPRO46
CPHE61
CPHE65
CLEU68
CCYS98
CCYS101
CHIS102
CTYR105
CARG106
DASP39
DHOH222

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM D 150
ChainResidue
CSER42
DGLU4
DMET7
DASN11
DPRO45
DPRO46
DPHE61
DPHE65
DLEU94
DCYS98
DCYS101
DHIS102
DARG106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues52
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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