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1OZL

Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

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 Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
ALYS18
AARG183
APHE207
AASN210
ANO1400
AHOH1460
AHIS25
AMET34
ATYR134
AGLY139
ASER142
AGLY143
ALEU147
ALYS179

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BLYS18
BHIS25
BGLU29
BMET34
BGLN38
BTYR134
BTHR135
BGLY139
BSER142
BARG183
BPHE207
BASN210
BNO5400
BHOH5445

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO A 1400
ChainResidue
AHIS25
AGLY139
AHEM300
AHOH1593

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NO B 5400
ChainResidue
BGLY139
BHEM300

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
AALA140
BALA140

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
AALA140
AGLY143
AHIS25
AGLY139

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BARG136
BTYR58
BTHR135
BALA140
BGLY143
BHIS25
BGLY139

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
AALA140
AGLY144

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dve
ChainResidueDetails
BALA140
BGLY144

226707

PDB entries from 2024-10-30

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