Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T42822 | Target Info | |||
| Target Name | Ferrochelatase (FECH) | ||||
| Synonyms | Protoheme ferro-lyase; Heme synthetase; FECH | ||||
| Target Type | Successful Target | ||||
| Gene Name | FECH | ||||
| Biochemical Class | Ferrochelatase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Protoporphyrin IX | Ligand Info | |||
| Canonical SMILES | CC1=C(C2=CC3=NC(=CC4=NC(=CC5=C(C(=C(N5)C=C1N2)C=C)C)C(=C4CCC(=O)O)C)C(=C3C)CCC(=O)O)C=C | ||||
| InChI | 1S/C34H34N4O4/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25/h7-8,13-16,35-36H,1-2,9-12H2,3-6H3,(H,39,40)(H,41,42) | ||||
| InChIKey | ZCFFYALKHPIRKJ-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 4971 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2QD1 2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [1] |
| PDB Sequence |
RKPKTGILML
74 NMGGPETLGD84 VHDFLLRLFL94 DRDLMTLPIQ104 NKLAPFIAKR114 RTPKIQEQYR 124 RIGGGSPIKI134 WTSKQGEGMV144 KLLDELSPNT154 APHKYYIGFR164 YVHPLTEEAI 174 EEMERDGLER184 AIAFTQYPQY194 SCSTTGSSLN204 AIYRYYNQVG214 RKPTMKWSTI 224 DRWPTHHLLI234 QCFADHILKE244 LDHFPLEKRS254 EVVILFSAHS264 LPMSVVNRGD 274 PYPQEVSATV284 QKVMERLEYC294 NPYRLVWQSK304 VGPMPWLGPQ314 TDESIKGLCE 324 RGRKNILLVP334 IAFTSDHIKT344 LYELDIEYSQ354 VLAKECGVEN364 IRRAESLNGN 374 PLFSKALADL384 VHSHIQSNEL394 CSKQLTLSCP404 LCVNPVCRET414 KSFFTSQQL |
|||||
|
|
ASN75
3.727
MET76
3.227
GLY77
3.561
GLY78
3.660
PHE88
3.578
LEU89
3.724
LEU92
3.395
PHE93
3.767
LEU98
3.237
MET99
3.776
ARG115
2.475
ILE119
3.013
GLN122
4.752
TYR123
2.672
SER130
2.645
ILE132
3.828
|
|||||
| PDB ID: 2QD5 Structure of wild type human ferrochelatase in complex with a lead-porphyrin compound | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] |
| PDB Sequence |
RKPKTGILML
74 NMGGPETLGD84 VHDFLLRLFL94 DRDLMTLPIQ104 NKLAPFIAKR114 RTPKIQEQYR 124 RIGGGSPIKI134 WTSKQGEGMV144 KLLDELSPNT154 APHKYYIGFR164 YVHPLTEEAI 174 EEMERDGLER184 AIAFTQYPQY194 SCSTTGSSLN204 AIYRYYNQVG214 RKPTMKWSTI 224 DRWPTHHLLI234 QCFADHILKE244 LDHFPLEKRS254 EVVILFSAHS264 LPMSVVNRGD 274 PYPQEVSATV284 QKVMERLEYC294 NPYRLVWQSK304 VGPMPWLGPQ314 TDESIKGLCE 324 RGRKNILLVP334 IAFTSDHIET344 LYELDIEYSQ354 VLAKECGVEN364 IRRAESLNGN 374 PLFSKALADL384 VHSHIQSNEL394 CSKQLTLSCP404 LCVNPVCRET414 KSFFTSQQL |
|||||
|
|
MET76
3.387
PHE88
4.246
LEU89
4.075
LEU92
3.736
PHE93
3.487
LEU98
3.599
MET99
4.265
ARG115
3.037
ILE119
3.157
TYR123
3.730
TYR191
4.208
SER195
3.666
SER197
3.445
THR198
3.722
|
|||||
| PDB ID: 2HRE Structure of human ferrochelatase variant E343K with protoporphyrin IX bound | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | Yes | [2] |
| PDB Sequence |
RKPKTGILML
74 NMGGPETLGD84 VHDFLLRLFL94 DRDLMTLPIQ104 NKLAPFIAKR114 RTPKIQEQYR 124 RIGGGSPIKI134 WTSKQGEGMV144 KLLDELSPNT154 APHKYYIGFR164 YVHPLTEEAI 174 EEMERDGLER184 AIAFTQYPQY194 SCSTTGSSLN204 AIYRYYNQVG214 RKPTMKWSTI 224 DRWPTHHLLI234 QCFADHILKE244 LDHFPLEKRS254 EVVILFSAHS264 LPMSVVNRGD 274 PYPQEVSATV284 QKVMERLEYC294 NPYRLVWQSK304 VGPMPWLGPQ314 TDESIKGLCE 324 RGRKNILLVP334 IAFTSDHIKT344 LYELDIEYSQ354 VLAKECGVEN364 IRRAESLNGN 374 PLFSKALADL384 VHSHIQSNEL394 CSKQLTLSCP404 LCVNPVCRET414 KSFFTSQQL |
|||||
|
|
ASN75
4.081
MET76
3.258
GLY77
3.582
GLY78
3.601
PRO79
4.787
PHE88
3.691
LEU89
3.596
LEU92
3.538
PHE93
3.704
LEU98
2.890
MET99
3.681
ARG115
2.317
ILE119
3.460
TYR123
2.277
SER130
2.608
ILE132
3.756
TYR191
3.537
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase. J Mol Biol. 2007 Nov 2;373(4):1006-16. | ||||
| REF 2 | Substrate interactions with human ferrochelatase. Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. | ||||
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