Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2QPP

Crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme

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 HEM A 300
ChainResidue
AHIS45
AARG203
APHE227
APHE234
AHOH319
AVAL54
ALEU58
ATYR154
ATHR155
AARG156
AGLY159
ASER162
ALYS199

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 300
ChainResidue
BHIS45
BVAL54
BLEU58
BTYR154
BTHR155
BARG156
BGLY159
BSER162
BLYS199
BARG203
BPHE227
BASN230
BPHE234

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYMG
ChainResidueDetails
ALEU149-GLY159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP
ChainResidueDetails
AHIS45
BHIS45

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP
ChainResidueDetails
ATYR154
ALYS199
AARG203
BTYR154
BLYS199
BARG203

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P09601
ChainResidueDetails
AASP160
BASP160

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2
BSER2

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon