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Crystal structure of heme oxygenase-2 from Synechocystis sp. PCC 6803 complexed with heme in ferrous form

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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
AARG9
AGLY133
AARG175
APHE199
AASN202
AARG230
AHIS242
AILE244
AHOH356
AHOH400
AHOH432
AHIS16
AHOH481
AGLU20
ALEU29
ATYR124
ATHR125
AARG126
AGLY129
ASER132

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BARG9
BHIS16
BGLU20
BLEU29
BTYR124
BTHR125
BARG126
BGLY129
BSER132
BGLY133
BLYS171
BARG175
BPHE199
BASN202
BSER233
BTHR234
BILE244
BHOH348
BHOH408

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LIAHCYTRYLG
ChainResidueDetails
ALEU119-GLY129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS16
BHIS16

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AARG126
AGLY133
ATYR49
AASP130
AHIS16
AGLY129
ATHR125

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BARG126
BGLY133
BTYR49
BASP130
BHIS16
BGLY129
BTHR125

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AGLY134
AASP130

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BGLY134
BASP130

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PDB entries from 2024-11-13

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