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1WZF

Crystal Structure Of An Artificial Metalloprotein: Fe(10-COOH-Salophen)/Wild Type Heme oxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042167biological_processheme catabolic process
A0046872molecular_functionmetal ion binding
B0004392molecular_functionheme oxygenase (decyclizing) activity
B0006788biological_processheme oxidation
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042167biological_processheme catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
ASER26
ATHR27
AHIS205
AHOH917

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AALA69
AGLU70
ASER71
AHOH926

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 703
ChainResidue
BTHR27
BHIS205
BHOH972
BHOH1008
BSER26

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE YOL A 901
ChainResidue
AHIS20
AALA23
AGLU24
ATYR130
AVAL131
AARG132
ALEU134
AGLY135
ASER138
AGLY139
AARG177
APHE201
AASN204
APHE208

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE YOL B 902
ChainResidue
BHIS20
BGLU24
BTYR130
BVAL131
BLEU134
BGLY135
BSER138
BGLY139
BARG177
BASN204
BPHE208

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 801
ChainResidue
AVAL39
AHIS150
ATYR151
BASN119
BASP121
BHIS192
BGLU196
BHOH945

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 site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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 2025-10-08

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