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1WZG

Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004392molecular_functionheme oxygenase (decyclizing) activity
B0006788biological_processheme oxidation
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AASN91
ASER93
AGLU95
ATRP96
AARG99
AHOH1049

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AHOH931
AHOH1095
ASER26
ATHR27
AHIS205

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 703
ChainResidue
BSER26
BTHR27
BHIS205
BHOH932

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 705
ChainResidue
ASER138
ALYS173
AARG177
AHOH1009

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 706
ChainResidue
AARG112
AHIS192
AHOH941

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE YOM A 901
ChainResidue
AHIS20
AGLU24
AVAL131
AARG132
ALEU134
AGLY135
ASER138
AGLY139
APHE201
AASN204
APHE208
AHOH1054

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE YOM B 902
ChainResidue
BHIS20
BGLU24
BVAL131
BGLY135
BSER138
BGLY139
BPHE201
BASN204
BPHE208

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 801
ChainResidue
AVAL39
ATYR151
BASN119
BASP121
BHIS192
BGLU196
BHOH1024

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHHYVRYLG
ChainResidueDetails
ALEU125-GLY135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
AHIS20
BHIS20

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1wnw
ChainResidueDetails
AASP136
AGLY140

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1wnw
ChainResidueDetails
BASP136
BGLY140

site_idMCSA1
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
AHIS25metal ligand
ATYR53activator, electrostatic stabiliser
AVAL131activator
AARG132activator
AGLY135steric role
AASP136modifies pKa
AGLY140steric role

site_idMCSA2
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
BHIS25metal ligand
BTYR53activator, electrostatic stabiliser
BVAL131activator
BARG132activator
BGLY135steric role
BASP136modifies pKa
BGLY140steric role

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PDB entries from 2024-07-24

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