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1N3U

Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B

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 Residues1
DetailsBINDING SITE FOR RESIDUE CL A 234
ChainResidue
ATHR176

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 234
ChainResidue
BTHR192

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 235
ChainResidue
BSER174

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
AGLY139
ALYS179
APHE207
AASN210
APHE214
AHOH301
ALYS18
AHIS25
AGLU29
AGLN38
ATYR134
ATHR135

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BLYS18
BHIS25
BGLU29
BGLN38
BTYR134
BTHR135
BGLY139
BLYS179
BPHE207
BASN210
BPHE214
BHOH301

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

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AARG136
ATYR58
ATHR135
AASP140
AGLY143
AHIS25
AGLY139

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BARG136
BTYR58
BTHR135
BASP140
BGLY143
BHIS25
BGLY139

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AASP140
AGLY144

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BASP140
BGLY144

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PDB entries from 2024-07-17

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