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 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
HEMH_HUMAN
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
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
NMGGPETLGD
84
VHDFLLRLFL
94
DRDLMTLPIQ
104
NKLAPAIAKR
114

RTPKIQEQYR
124
RIGGGSPIKI
134
WTSKQGEGMV
144
KLLDELSPNT
154
APHKYYIGFR
164

YVHPLTEEAI
174
EEMERDGLER
184
AIAFTQYPQY
194
SCSTTGSSLN
204
AIYRYYNQVG
214

RKPTMKWSTI
224
DRWPTHHLLI
234
QCFADHILKE
244
LDHFPLEKRS
254
EVVILFSAHS
264

LPMSVVNRGD
274
PYPQEVSATV
284
QKVMERLEYC
294
NPYRLVWQSK
304
VGPMPWLGPQ
314

TDESIKGLCE
324
RGRKNILLVP
334
IAFTSDHIET
344
LYELDIEYSQ
354
VLAKECGVEN
364

IRRAESLNGN
374
PLFSKALADL
384
VHSHIQSNEL
394
CSKQLTLSCP
404
LCVNPVCRET
414

KSFFTSQQL
Residue
Distance (Å)
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
Residue
Distance (Å)
SER195
4.425
SER197
3.671
THR198
3.542
HIS263
3.454
SER264
4.126
LEU265
3.484
PRO266
3.654
VAL269
4.867
TYR276
3.505
VAL305
3.830
TRP310
4.087
PHE337
3.829
HIS341
4.088
ILE342
3.539
GLU343
3.458
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
NMGGPETLGD
84
VHDFLLRLFL
94
DRDLMTLPIQ
104
NKLAPFIAKR
114

RTPKIQEQYR
124
RIGGGSPIKI
134
WTSKQGEGMV
144
KLLDELSPNT
154
APHKYYIGFR
164

YVHPLTEEAI
174
EEMERDGLER
184
AIAFTQYPQY
194
SCSTTGSSLN
204
AIYRYYNQVG
214

RKPTMKWSTI
224
DRWPTHHLLI
234
QCFADHILKE
244
LDHFPLEKRS
254
EVVILFSAHS
264

LPMSVVNRGD
274
PYPQEVSATV
284
QKVMERLEYC
294
NPYRLVWQSK
304
VGPMPWLGPQ
314

TDESIKGLCE
324
RGRKNILLVP
334
IAFTSDHIET
344
LYELDIEYSQ
354
VLAKECGVEN
364

IRRAESLNGN
374
PLFSKALADL
384
VHSHIQSNEL
394
CSKQLTLSCP
404
LCVNPVCRET
414

KSFFTSQQL
Residue
Distance (Å)
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
Residue
Distance (Å)
THR198
3.523
HIS263
3.490
SER264
4.200
LEU265
3.521
PRO266
3.820
TYR276
3.641
SER303
4.314
VAL305
3.718
TRP310
3.903
PHE337
3.726
HIS341
3.151
ILE342
2.989
References  Top
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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