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1WNX

D136E 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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ASER26
ATHR27
AHOH3047

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BARG112
BHIS192
BHOH1079

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AARG97
AHOH3027
AHOH3115
AHOH3124
BHOH1099
AGLN14
AGLU81
AALA84

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AGLN58
ALYS173
AARG177
AHEM901
AHOH3138

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
AALA69
AGLU70
ASER71
AHOH3048
AHOH3058
AHOH3068
BLYS168

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1006
ChainResidue
ALEU169
ALYS170

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1007
ChainResidue
ATHR101
ASER103
BTHR27
BHOH1072
BHOH1143

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1008
ChainResidue
BPRO75
BALA76
BASN78
BHOH1159

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1009
ChainResidue
AHIS162
BASN91
BSER93
BGLU95
BTRP96
BARG99

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1010
ChainResidue
BALA69
BGLU70
BSER71
BHOH1025
BHOH1034
BHOH1141

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1011
ChainResidue
BGLN58
BARG177
BHOH1119
BHOH1138

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 3001
ChainResidue
AGLU115
BVAL39
BALA40
BHOH1182

site_idBC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 901
ChainResidue
ALYS13
AHIS20
AGLU24
ALEU33
AARG117
ATYR130
AVAL131
AGLY135
ASER138
AVAL142
ALYS173
AARG177
APHE201
AASN204
APHE208
ASO41004
AHOH3005
AHOH3017
AHOH3107
AHOH3138

site_idBC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 902
ChainResidue
BLYS13
BHIS20
BGLN58
BTYR130
BVAL131
BGLY135
BSER138
BARG177
BPHE201
BPHE208
BHOH1032
BHOH1059
BHOH1091
BHOH1196

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
AGLU136
AGLY140

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1wnw
ChainResidueDetails
BGLU136
BGLY140

site_idMCSA1
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
AHIS25metal ligand
ATYR53activator, electrostatic stabiliser
AVAL131activator
AARG132activator
AGLY135steric role
AGLU136modifies pKa
AGLY140steric role

site_idMCSA2
Number of Residues7
DetailsM-CSA 795
ChainResidueDetails
BHIS25metal ligand
BTYR53activator, electrostatic stabiliser
BVAL131activator
BARG132activator
BGLY135steric role
BGLU136modifies pKa
BGLY140steric role

226707

PDB entries from 2024-10-30

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