Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1WNW

D136N mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)

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
C0004392molecular_functionheme oxygenase (decyclizing) activity
C0006788biological_processheme oxidation
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0042167biological_processheme catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD C 1001
ChainResidue
CTRP96

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD B 1002
ChainResidue
BMET29
BHEM902
BHOH4097

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 1003
ChainResidue
BASP154

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 1006
ChainResidue
AIOD1007
AHOH2083
AHOH2132

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 1007
ChainResidue
AIOD1006
AHOH2032
AHEM901

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1008
ChainResidue
AHOH2127

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 4001
ChainResidue
BASP108
BGLN206

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 4002
ChainResidue
BHOH4062
BHOH4157

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2001
ChainResidue
CVAL82
CARG85
CGLY159
CHOH2091

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2002
ChainResidue
CTYR161
CHIS162
CPHE163
CLEU169

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2003
ChainResidue
BSER26
BTHR27
BHIS205
BHOH4105

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2004
ChainResidue
BVAL82
BARG85
BGLY159
BHOH4017

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2005
ChainResidue
BLYS170
BLYS173
BARG177
BHOH4078

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2006
ChainResidue
AVAL202
BGLY165
BILE166
BALA167

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2007
ChainResidue
APRO123
AGLU188
AGLN189
AHIS192
AHOH2104

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2008
ChainResidue
BARG44
BARG99
BHOH4111

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2009
ChainResidue
AARG97
AHOH2016
AHOH2137

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 2010
ChainResidue
CLYS89
CLEU90
CGLY152
CVAL153
CASP154
CALA157

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2011
ChainResidue
ALYS13
ALYS173
AARG177
AHOH2077

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 2012
ChainResidue
BHOH4035
BHOH4053
CHOH2059

site_idCC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ALYS13
AHIS20
AALA23
AGLU24
ALEU33
ATYR130
AVAL131
AGLY135
ASER138
AGLY139
AARG177
AASN204
APHE208
AIOD1007
AHOH2033
AHOH2126
AHOH2138

site_idCC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 902
ChainResidue
BLYS13
BHIS20
BALA23
BLEU33
BTYR130
BVAL131
BGLY135
BSER138
BARG177
BPHE201
BASN204
BPHE208
BIOD1002
BHOH4010
BHOH4078
BHOH4159

site_idCC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM C 903
ChainResidue
CALA23
CLEU33
CTYR130
CVAL131
CGLY135
CSER138
CARG177
CPHE201
CASN204
CHOH2062
CHOH2085
CLYS13
CHIS20

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 Residues3
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
AHIS20
BHIS20
CHIS20

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
AHIS25metal ligand
ATYR53activator, electrostatic stabiliser
AVAL131activator
AARG132activator
AGLY135steric role
AASN136modifies pKa
AGLY140steric role

site_idMCSA2
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
BHIS25metal ligand
BTYR53activator, electrostatic stabiliser
BVAL131activator
BARG132activator
BGLY135steric role
BASN136modifies pKa
BGLY140steric role

site_idMCSA3
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
CHIS25metal ligand
CTYR53activator, electrostatic stabiliser
CVAL131activator
CARG132activator
CGLY135steric role
CASN136modifies pKa
CGLY140steric role

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon