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1WE1

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
A0006979biological_processresponse to oxidative stress
A0015979biological_processphotosynthesis
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
B0015979biological_processphotosynthesis
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
C0015979biological_processphotosynthesis
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0042167biological_processheme catabolic process
C0046872molecular_functionmetal ion binding
D0004392molecular_functionheme oxygenase (decyclizing) activity
D0006788biological_processheme oxidation
D0006979biological_processresponse to oxidative stress
D0015979biological_processphotosynthesis
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0042167biological_processheme catabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 241
ChainResidue
ALYS165
ALYS168
DLYS165
DLYS168
DARG172

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 241
ChainResidue
CLYS168
CARG172
BLYS165
BLYS168
BARG172
CLYS165

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 242
ChainResidue
BLYS14

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 241
ChainResidue
CARG10

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 243
ChainResidue
AARG108
AASP194

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
AARG10
AHIS17
AALA20
ALEU30
ATYR125
ATHR126
AGLY130
ASER133
AILE137
ALEU138
ALYS168
AARG172
APHE203
AHOH1006
DLYS165

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BARG10
BHIS17
BALA20
BVAL26
BLEU30
BTYR125
BTHR126
BGLY130
BSER133
BGLY134
BLEU138
BPHE196
BASN199
BHOH1007
BHOH1051
CLYS165

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM C 300
ChainResidue
BLYS165
CARG10
CHIS17
CALA20
CVAL26
CTYR125
CTHR126
CGLY130
CSER133
CILE137
CLEU138
CPHE196
CASN199
CHOH1008
CHOH1011
CHOH1012

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM D 300
ChainResidue
ALYS165
DARG10
DHIS17
DALA20
DVAL26
DLEU30
DTYR125
DTHR126
DARG127
DGLY130
DSER133
DILE137
DARG172
DPHE196
DASN199
DPHE203
DHOH1009

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA D 1004
ChainResidue
DTYR156
DPHE203

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA C 1003
ChainResidue
CTYR156
CHOH1072

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IPA B 1002
ChainResidue
BPHE203

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA A 1001
ChainResidue
APHE29
ALEU42

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IPA A 1005
ChainResidue
AGLU54
AMET57
AILE69
ATYR70
APHE71
AASN75
ATYR128

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IPA B 1006
ChainResidue
BTYR128
BMET57
BILE69
BTYR70
BPHE71
BLEU74
BSER124

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA C 1007
ChainResidue
CMET57
CILE69
CPHE71
CLEU74
CASN75
CSER124

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IPA D 1008
ChainResidue
DMET57
DILE69
DTYR70
DPHE71
DASN75
DSER124
DTYR128

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHSYTRYLG
ChainResidueDetails
ALEU120-GLY130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS17
BHIS17
CHIS17
DHIS17

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
ATHR126
AHIS17
AASP131
AGLY134
AARG127
AGLY130
ATYR50

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BTHR126
BHIS17
BASP131
BGLY134
BARG127
BGLY130
BTYR50

site_idCSA3
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
CTHR126
CHIS17
CASP131
CGLY134
CARG127
CGLY130
CTYR50

site_idCSA4
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
DTHR126
DHIS17
DASP131
DGLY134
DARG127
DGLY130
DTYR50

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AGLY135
AASP131

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BGLY135
BASP131

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
CGLY135
CASP131

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
DGLY135
DASP131

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PDB entries from 2024-07-31

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