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6DYG

Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue HEC A 201
ChainResidue
AMET7
APHE61
APHE65
ACYS98
ACYS101
AHIS102
ATYR105
AARG106

site_idAC2
Number of Residues6
Detailsbinding site for residue FE A 202
ChainResidue
AHIS71
AHIS97
AHOH363
BHIS67
BHIS71
AHIS67

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 202
ChainResidue
BGLU4
BHEC201

site_idAC4
Number of Residues23
Detailsbinding site for Di-peptide HEC B 201 and CYS B 101
ChainResidue
BGLU4
BMET7
BGLU8
BASN11
BMET33
BPRO45
BPRO46
BPHE61
BGLY64
BPHE65
BHIS97
BCYS98
BASN99
BALA100
BHIS102
BGLN103
BLYS104
BTYR105
BARG106
BMG202
BHOH304
BHOH312
BHOH326

site_idAC5
Number of Residues24
Detailsbinding site for Di-peptide HEC B 201 and CYS B 98
ChainResidue
BGLU4
BMET7
BGLU8
BASN11
BMET33
BPRO45
BPRO46
BPHE61
BGLY64
BPHE65
BLEU94
BLYS95
BCYS96
BHIS97
BASN99
BALA100
BCYS101
BHIS102
BTYR105
BARG106
BMG202
BHOH304
BHOH312
BHOH326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
AMET7
AHIS102
BMET7
BHIS102

218853

PDB entries from 2024-04-24

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