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1LM3

A Multi-generation Analysis of Cytochrome b562 Redox Variants: Evolutionary Strategies for Modulating Redox Potential Revealed Using a Library Approach

Functional Information from GO Data
ChainGOidnamespacecontents
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_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 Residues2
DetailsBINDING SITE FOR RESIDUE MG B 107
ChainResidue
BASP5
BTHR9

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 107
ChainResidue
DASP74

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BILE61
BTYR65
BLEU68
BARG98
BHIS102
BLEU106
BHOH205
DASN22
DALA23
BLEU3
BGLU4
BMET7
BLEU10
BASN11
BPRO46

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM D 200
ChainResidue
BASN22
BALA23
BGLY82
DGLU4
DMET7
DLEU10
DASN11
DPRO46
DILE61
DTYR65
DLEU68
DARG98
DTYR101
DHIS102
DTYR105
DHOH210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
BMET7
BHIS102
DMET7
DHIS102

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PDB entries from 2024-10-16

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