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1XK3

NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
B0004392molecular_functionheme oxygenase (decyclizing) activity
B0006788biological_processheme oxidation
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
ALYS18
ALEU147
ALYS179
APHE207
AASN210
APHE214
ANO400
AHOH454
AHIS25
AMET34
AGLN38
ATYR134
ATHR135
AARG136
AGLY139
ASER142

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BLYS18
BHIS25
BGLU29
BMET34
BGLN38
BTYR134
BTHR135
BARG136
BGLY139
BLEU147
BGLU183
BPHE207
BASN210
BPHE214
BHOH371

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO A 400
ChainResidue
AGLY139
AHEM300
AHOH418

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYLG
ChainResidueDetails
ALEU129-GLY139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW
ChainResidueDetails
AGLU183
BLYS18
BTYR134
BGLU183
ALYS18
ATYR134

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW
ChainResidueDetails
AHIS25
BHIS25

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:11121422
ChainResidueDetails
AASP140
BASP140

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER229
BSER229

221051

PDB entries from 2024-06-12

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