Target Binding Site Detail
Target General Information | Top | ||||
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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 | FE(III) Deuteroporphyrin IX | Ligand Info | |||
Canonical SMILES | CC1=CC2=CC3=NC(=CC4=C(C(=C([N-]4)C=C5C(=C(C(=N5)C=C1[N-]2)C)CCC(=O)O)CCC(=O)O)C)C=C3C.[Fe+2] | ||||
InChI | 1S/C30H30N4O4.Fe/c1-15-9-20-12-25-17(3)21(5-7-29(35)36)27(33-25)14-28-22(6-8-30(37)38)18(4)26(34-28)13-24-16(2)10-19(32-24)11-23(15)31-20;/h9-14H,5-8H2,1-4H3,(H4,31,32,33,34,35,36,37,38);/q;+2/p-2 | ||||
InChIKey | QQYZTXBVPVYDJC-UHFFFAOYSA-L | ||||
PubChem Compound ID | 9547898 |
Drug Binding Sites of Target | Top | |||||
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PDB ID: 3HCP Human ferrochelatase with Mn and deuteroporphyrin bound | ||||||
Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [1] |
PDB Sequence |
RKPKTGILML
74 NMGGPETLGD84 VHDFLLRLFL94 DRDLMTLPIQ104 NKLAPAIAKR114 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 |
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|
MET76
3.511
GLY77
4.913
GLY78
4.450
PRO79
3.814
PHE88
3.358
LEU89
4.228
LEU92
3.891
PHE93
3.591
LEU98
3.613
MET99
3.672
ARG115
2.688
LYS118
4.765
ILE119
3.544
GLN122
4.993
TYR123
2.205
|
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PDB ID: 3HCR Human Ferrochelatase with deuteroporphyrin and Ni Bound | ||||||
Method | X-ray diffraction | Resolution | 2.20 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 |
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|
MET76
3.319
PHE88
4.342
LEU89
3.846
LEU92
3.925
PHE93
3.717
LEU98
3.774
MET99
4.340
ARG115
2.534
ILE119
3.655
TYR123
3.644
SER195
4.263
SER197
3.430
|
References | Top | ||||
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REF 1 | Product release rather than chelation determines metal specificity for ferrochelatase. J Mol Biol. 2009 Oct 23;393(2):308-19. |
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