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 T11843 Target Info
Target Name Vitamin K epoxide reductase complex 1 (VKORC1)
Synonyms Vitamin K1 2,3-epoxide reductase subunit 1; VKORC1; VKOR; UNQ308/PRO351; MSTP576; MSTP134
Target Type Successful Target
Gene Name VKORC1
Biochemical Class Short-chain dehydrogenases reductase
UniProt ID
VKOR1_HUMAN
Ligand General Information  Top
Ligand Name Warfarin Ligand Info
Canonical SMILES CC(=O)CC(C1=CC=CC=C1)C2=C(C3=CC=CC=C3OC2=O)O
InChI 1S/C19H16O4/c1-12(20)11-15(13-7-3-2-4-8-13)17-18(21)14-9-5-6-10-16(14)23-19(17)22/h2-10,15,21H,11H2,1H3/t15-/m0/s1
InChIKey PJVWKTKQMONHTI-HNNXBMFYSA-N
PubChem Compound ID 54688261
Drug Binding Sites of Target  Top
PDB ID: 6WV3      Human VKOR with warfarin
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [1]
PDB Sequence
KGEELFTGVV
12
PILVELDGDV
22
NGHKFSVRGE
32
GEGDATNGKL
42
TLKFICTTGK
52

LPVPWPTLVT
62
TLVQCFSRYP
75
DHMKRHDFFK
85
SAMPEGYVQE
95
RTISFKDDGT
105

YKTRAEVKFE
115
GDTLVNRIEL
125
KGIDFKEDGN
135
ILGHKLEYNS
145
TWGSPGWVRL
155

ALCLTGLVLS
165
LYALHVKAAR
175
ARDRDYRALC
185
DVGTAISCSR
195
VFSSRWGRGF
205

GLVEHVLGQD
215
SILNQSNSIF
225
GCIFYTLQLL
235
LGCLRTRWAS
245
VLMLLSSLVS
255

LAGSVYLAWI
265
LFFVLYDFCI
275
VCITTYAINV
285
SLMWLSFRKV
295
QENSHNVYIT
305

ADKQKNGIKA
315
NFKIRHNVED
325
GSVQLADHYQ
335
QNTPIGDGPV
345
LLPDNHYLST
355

QSVLSKDPNE
365
KRDHMVLLEF
375
VTAAGITHHH
385
Residue
Distance (Å)
LEU164
4.218
SER165
4.752
ALA168
3.667
VAL196
3.542
PHE197
3.701
SER199
3.864
TRP201
3.714
GLY202
3.730
PHE205
3.760
ASN222
2.762
SER223
3.938
Residue
Distance (Å)
SER259
3.584
LEU262
3.207
ALA263
4.972
ILE265
3.761
LEU266
3.746
LEU270
3.708
VAL276
3.320
CYS277
3.409
THR280
3.107
TYR281
2.462
ASN284
3.967
PDB ID: 6WV4      Human VKOR C43S with warfarin
Method X-ray diffraction Resolution 3.01 Å Mutation Yes [1]
PDB Sequence
SKGEELFTGV
11
VPILVELDGD
21
VNGHKFSVRG
31
EGEGDATNGK
41
LTLKFICTGK
52

LPVPWPTLVT
62
TLVQCFSRYP
75
DHMKRHDFFK
85
SAMPEGYVQE
95
RTISFKDDGT
105

YKTRAEVKFE
115
GDTLVNRIEL
125
KGIDFKEDGN
135
ILGHKLEYNS
145
TWGSPGWVRL
155

ALCLTGLVLS
165
LYALHVKAAG
188
TAISCSRVFS
198
SRWGRGFGLV
208
EHVLGQDSIL
218

NQSNSIFGCI
228
FYTLQLLLGC
238
LRTRWASVLM
248
LLSSLVSLAG
258
SVYLAWILFF
268

VLYDFCIVCI
278
TTYAINVSLM
288
WLSFRKVQEN
298
SHNVYITADK
308
QKNGIKANFK
318

IRHNVEDGSV
328
QLADHYQQNT
338
PIGDGPVLLP
348
DNHYLSTQSV
358
LSKDPNEKRD
368

HMVLLEFVTA
378
AGI
Residue
Distance (Å)
LEU164
4.703
SER165
4.166
ALA168
4.676
VAL196
3.515
PHE197
3.523
SER199
3.578
TRP201
3.473
GLY202
3.301
PHE205
3.682
ASN222
2.634
SER223
4.180
Residue
Distance (Å)
GLY258
4.985
SER259
4.098
LEU262
3.481
ILE265
4.212
LEU266
4.608
LEU270
4.263
VAL276
3.609
CYS277
3.182
THR280
3.570
TYR281
2.683
ASN284
3.906
References  Top
REF 1 Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science. 2021 Jan 1;371(6524):eabc5667.

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