Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1WZD

Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AARG112
AHIS192
AHOH978

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 702
ChainResidue
BSER26
BTHR27
BHIS205
BHOH960
BHOH976

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
AHOH1122
AHOH1143
AGLN58

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
AGLN58
AHOH936
AHOH951
AHOH1011

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 705
ChainResidue
BASP61
BGOL804
BHOH955
BHOH998
BHOH1075

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 706
ChainResidue
ASER26
ATHR27
AHIS205
AHOH931
AHOH1118

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE YOK A 901
ChainResidue
ALYS13
AHIS20
AGLU24
ATYR130
AVAL131
AARG132
AGLY135
ASER138
AGLY139
AARG177
APHE201
AASN204
APHE208
AHOH971
AHOH990
AHOH1116

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE YOK B 902
ChainResidue
BHIS20
BGLU24
BVAL131
BGLY135
BSER138
BGLY139
BLYS173
BARG177
BPHE201
BASN204
BPHE208
BHOH957
BHOH990
BHOH1084
BHOH1101

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 801
ChainResidue
BALA9
BLYS13
BARG177
BHOH1022
BHOH1101

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 802
ChainResidue
ASER94
AGLU95
ASER98
AHOH1021

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 803
ChainResidue
BSER30
BLYS34
BHOH918
BHOH1145

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 804
ChainResidue
BSO4705

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
APRO75
AASN78
AGLU81
AHOH943

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

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon