Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T25703 Target Info
Target Name Heme oxygenase 1 (HMOX1)
Synonyms HO1; HO-1; HO
Target Type Clinical trial Target
Gene Name HMOX1
Biochemical Class Paired donor oxygen oxidoreductase
UniProt ID
HMOX1_HUMAN
Ligand General Information  Top
Ligand Name Biliverdine Ix Alpha Ligand Info
Canonical SMILES CC1=C(C(=CC2=C(C(=C(N2)C=C3C(=C(C(=O)N3)C)C=C)C)CCC(=O)O)NC1=CC4=NC(=O)C(=C4C)C=C)CCC(=O)O
InChI 1S/C33H34N4O6/c1-7-20-19(6)32(42)37-27(20)14-25-18(5)23(10-12-31(40)41)29(35-25)15-28-22(9-11-30(38)39)17(4)24(34-28)13-26-16(3)21(8-2)33(43)36-26/h7-8,13-15,34-35H,1-2,9-12H2,3-6H3,(H,37,42)(H,38,39)(H,40,41)/b24-13-,27-14-,28-15-
InChIKey RCNSAJSGRJSBKK-NSQVQWHSSA-N
PubChem Compound ID 5280353
Drug Binding Sites of Target  Top
PDB ID: 5BTQ      Crystal structure of human heme oxygenase 1 H25R with biliverdin bound
Method X-ray diffraction Resolution 2.08 Å Mutation Yes [1]
PDB Sequence
QDLSEALKEA
20
TKEVRTQAEN
30
AEFMRNFQKG
40
QVTRDGFKLV
50
MASLYHIYVA
60

LEEEIERNKE
70
SPVFAPVYFP
80
EELHRKAALE
90
QDLAFWYGPR
100
WQEVIPYTPA
110

MQRYVKRLHE
120
VGRTEPELLV
130
AHAYTRYLGD
140
LSGGQVLKKI
150
AQKALDLPSS
160

GEGLAFFTFP
170
NIASATKFKQ
180
LYRSRMNSLE
190
MTPAVRQRVI
200
EEAKTAFLLN
210

IQLFEELQEL
220
LTH
Residue
Distance (Å)
SER14
4.372
LYS18
3.839
ARG25
3.171
ALA28
3.516
GLU29
3.448
MET34
3.684
GLN38
3.911
TYR134
2.900
THR135
3.763
ARG136
4.512
LEU138
3.982
Residue
Distance (Å)
GLY139
3.166
ASP140
4.181
SER142
3.201
GLY143
3.542
LEU147
3.330
LYS179
4.010
ARG183
3.135
PHE207
3.377
ASN210
3.473
PHE214
3.966
PDB ID: 1S8C      Crystal structure of human heme oxygenase in a complex with biliverdine
Method X-ray diffraction Resolution 2.19 Å Mutation No [2]
PDB Sequence
PQDLSEALKE
19
ATKEVHTQAE
29
NAEFMRNFQK
39
GQVTRDGFKL
49
VMASLYHIYV
59

ALEEEIERNK
69
ESPVFAPVYF
79
PEELHRKAAL
89
EQDLAFWYGP
99
RWQEVIPYTP
109

AMQRYVKRLH
119
EVGRTEPELL
129
VAHAYTRYLG
139
DLSGGQVLKK
149
IAQKALDLPS
159

SGEGLAFFTF
169
PNIASATKFK
179
QLYRSRMNSL
189
EMTPAVRQRV
199
IEEAKTAFLL
209

NIQLFEELQE
219
LLTH
Residue
Distance (Å)
HIS25
4.219
ALA28
3.803
GLU29
3.563
MET34
3.505
PHE37
4.537
GLN38
2.321
LEU49
4.677
VAL50
3.439
SER53
3.284
LEU54
3.669
ILE57
3.075
TYR114
3.731
HIS132
4.292
THR135
2.369
ARG136
2.294
TYR137
4.614
GLY139
3.477
Residue
Distance (Å)
ASP140
2.346
LEU141
4.513
SER142
4.898
GLY143
2.610
GLY144
2.433
GLN145
4.853
VAL146
4.658
LEU147
2.339
PHE166
2.618
PHE167
3.326
ALA206
3.812
PHE207
3.219
ASN210
2.402
LEU213
3.212
PHE214
3.577
LEU217
3.626
References  Top
REF 1 In-Cell Enzymology To Probe His-Heme Ligation in Heme Oxygenase Catalysis. Biochemistry. 2016 Aug 30;55(34):4836-49.
REF 2 Crystal structure of human heme oxygenase-1 in a complex with biliverdin. Biochemistry. 2004 Apr 6;43(13):3793-801.

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