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5BTQ

Crystal structure of human heme oxygenase 1 H25R with biliverdin bound

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 Residues13
Detailsbinding site for residue BLA A 301
ChainResidue
AARG25
AARG183
APHE207
AASN210
AHOH403
AALA28
AGLU29
AMET34
ATYR134
AGLY139
ASER142
AGLY143
ALEU147

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 302
ChainResidue
ASER174
AALA175
ATHR176

site_idAC3
Number of Residues14
Detailsbinding site for residue BLA B 301
ChainResidue
BLYS18
BARG25
BALA28
BGLU29
BMET34
BGLN38
BTYR134
BGLY139
BSER142
BGLY143
BLEU147
BARG183
BPHE207
BPHE214

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
AARG25
BARG25

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

219140

PDB entries from 2024-05-01

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