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3TGM

X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(1H-imidazol-1-yl)-4,4-diphenyl-2 butanone

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 Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
AHIS25
APHE207
AASN210
A3TG301
AGLU29
AMET34
AGLN38
ATYR134
ATHR135
AGLY139
ALYS179
AARG183

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3TG A 301
ChainResidue
APHE37
AVAL50
AARG136
AGLY139
AASP140
AGLY143
ALEU147
APHE167
AASN210
APHE214
AHEM300

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BHIS25
BMET34
BTYR134
BTHR135
BGLY139
BARG183
BPHE207
BASN210
BPHE214
B3TG301

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3TG B 301
ChainResidue
BMET34
BVAL50
BARG136
BGLY139
BASP140
BGLY143
BLEU147
BPHE167
BASN210
BPHE214
BHEM300

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HEZ A 234
ChainResidue
AGLU62
AGLU66
AVAL77
APHE79
APRO80
AHIS84
ATYR137

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
ALYS18
ATYR134
AARG183
BLYS18
BTYR134
BARG183

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

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PDB entries from 2024-10-16

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