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6DY4

Fe(II)-bound structure of the engineered cyt cb562 variant, CH2E

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
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 Residues6
Detailsbinding site for residue FE A 201
ChainResidue
AASP74
AHOH314
AHOH315
DHIS63
DHIS67
DHOH381

site_idAC2
Number of Residues16
Detailsbinding site for residue HEC A 202
ChainResidue
AASN11
AMET33
APRO45
APRO46
APHE61
APHE65
ACYS98
ACYS101
AHIS102
ATYR105
AARG106
AHOH303
AHOH319
AGLU4
AMET7
AGLU8

site_idAC3
Number of Residues6
Detailsbinding site for residue FE D 201
ChainResidue
AHIS67
AHIS71
AHOH306
DHIS71
DGLU97
DHOH342

site_idAC4
Number of Residues23
Detailsbinding site for Di-peptide HEC D 202 and CYS D 101
ChainResidue
DGLU4
DMET7
DASN11
DMET33
DPRO45
DPRO46
DPHE61
DGLY64
DPHE65
DGLU97
DCYS98
DASN99
DALA100
DHIS102
DGLN103
DLYS104
DTYR105
DARG106
DHOH311
DHOH321
DHOH325
DHOH358
DHOH363

site_idAC5
Number of Residues24
Detailsbinding site for Di-peptide HEC D 202 and CYS D 98
ChainResidue
AASP54
DGLU4
DMET7
DASN11
DMET33
DPRO45
DPRO46
DPHE61
DGLY64
DPHE65
DLEU94
DLYS95
DCYS96
DGLU97
DASN99
DALA100
DCYS101
DHIS102
DARG106
DHOH311
DHOH321
DHOH325
DHOH358
DHOH363

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
AMET7
AHIS102
DMET7
DHIS102

222036

PDB entries from 2024-07-03

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