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

1WOW

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

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon