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3HNL

Crystal structure of the Cu-induced dimer of the engineered cyt cb562 variant RIDC-1

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 Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 150
ChainResidue
ALEU3
APHE65
ACYS98
ACYS101
AHIS102
AARG106
AHOH117
AHOH199
BARG106
BHOH138
BHOH161
AMET7
AGLU8
ALEU10
AASN11
AMET33
APRO45
APHE61
AGLY64

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 107
ChainResidue
AHIS73
AHIS77
AHOH226
BHIS63
BGLU81

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 108
ChainResidue
AALA23
AHOH206
BVAL84
BLYS85

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 109
ChainResidue
AHOH117
AHOH118
AHOH203

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 150
ChainResidue
AARG106
AHOH123
AHOH125
BGLU4
BMET7
BLEU14
BMET33
BPRO45
BPRO46
BPHE61
BPHE65
BCYS98
BCYS101
BHIS102
BARG106
BHOH164
BHOH178
BHOH193

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU B 107
ChainResidue
AHIS63
AGLU81
AHOH202
BHIS73
BHIS77
BHOH180

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

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PDB entries from 2024-07-31

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