eF-site ID 6dwd-C
PDB Code 6dwd
Chain C

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Title SAMHD1 Bound to Clofarabine-TP in the Catalytic Pocket and Allosteric Pocket
Classification hydrolase/hydrolase inhibitor
Compound Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Source (SAMH1_HUMAN)
Sequence C:  DTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGG
GYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQIS
ERDVLCVQIAGLCRNLGHGPFSHMFDGRFIPLARPEVKWT
HEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQI
VGPLELWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFAR
DCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGN
LYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIE
ITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKL
KDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPK
EVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHV
SFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVD
RKSLYAARQYFVQWCADRNFTKPQDGDVIAPLITPQKKEW
N
Description


Functional site
1) chain C
residue 117
type
sequence V
description binding site for residue HDV D 703
source : AC3
2) chain C
residue 119
type
sequence N
description binding site for residue HDV D 703
source : AC3
3) chain C
residue 523
type
sequence K
description binding site for residue GTP D 704
source : AC4
4) chain C
residue 149
type
sequence Q
description binding site for residue HDV C 701
source : AD6
5) chain C
residue 150
type
sequence L
description binding site for residue HDV C 701
source : AD6
6) chain C
residue 164
type
sequence R
description binding site for residue HDV C 701
source : AD6
7) chain C
residue 206
type
sequence R
description binding site for residue HDV C 701
source : AD6
8) chain C
residue 210
type
sequence H
description binding site for residue HDV C 701
source : AD6
9) chain C
residue 215
type
sequence H
description binding site for residue HDV C 701
source : AD6
10) chain C
residue 233
type
sequence H
description binding site for residue HDV C 701
source : AD6
11) chain C
residue 311
type
sequence D
description binding site for residue HDV C 701
source : AD6
12) chain C
residue 312
type
sequence K
description binding site for residue HDV C 701
source : AD6
13) chain C
residue 315
type
sequence Y
description binding site for residue HDV C 701
source : AD6
14) chain C
residue 319
type
sequence D
description binding site for residue HDV C 701
source : AD6
15) chain C
residue 366
type
sequence R
description binding site for residue HDV C 701
source : AD6
16) chain C
residue 374
type
sequence Y
description binding site for residue HDV C 701
source : AD6
17) chain C
residue 375
type
sequence Q
description binding site for residue HDV C 701
source : AD6
18) chain C
residue 155
type
sequence Y
description binding site for residue GTP C 702
source : AD7
19) chain C
residue 156
type
sequence V
description binding site for residue GTP C 702
source : AD7
20) chain C
residue 378
type
sequence V
description binding site for residue GTP C 702
source : AD7
21) chain C
residue 451
type
sequence R
description binding site for residue GTP C 702
source : AD7
22) chain C
residue 455
type
sequence K
description binding site for residue GTP C 702
source : AD7
23) chain C
residue 116
type
sequence K
description binding site for residue MG C 703
source : AD8
24) chain C
residue 330
type
sequence D
description binding site for residue HDV C 704
source : AD9
25) chain C
residue 333
type
sequence R
description binding site for residue HDV C 704
source : AD9
26) chain C
residue 352
type
sequence R
description binding site for residue HDV C 704
source : AD9
27) chain C
residue 354
type
sequence K
description binding site for residue HDV C 704
source : AD9
28) chain C
residue 358
type
sequence N
description binding site for residue HDV C 704
source : AD9
29) chain C
residue 523
type
sequence K
description binding site for residue HDV C 704
source : AD9
30) chain C
residue 164
type
sequence R
description binding site for residue MG C 707
source : AE3
31) chain C
residue 167
type
sequence H
description binding site for residue MG C 707
source : AE3
32) chain C
residue 207
type
sequence N
description binding site for residue MG C 707
source : AE3
33) chain C
residue 311
type
sequence D
description binding site for residue MG C 707
source : AE3
34) chain C
residue 334
type
sequence F
description binding site for residue NA C 708
source : AE4
35) chain C
residue 355
type
sequence E
description binding site for residue NA C 708
source : AE4
36) chain C
residue 357
type
sequence G
description binding site for residue NA C 709
source : AE5
37) chain C
residue 358
type
sequence N
description binding site for residue NA C 709
source : AE5
38) chain C
residue 361
type
sequence D
description binding site for residue NA C 709
source : AE5
39) chain C
residue 247
type
sequence S
description binding site for residue NA C 710
source : AE6
40) chain C
residue 248
type
sequence N
description binding site for residue NA C 710
source : AE6
41) chain C
residue 292
type
sequence E
description binding site for residue NA C 711
source : AE7
42) chain C
residue 452
type
sequence N
description binding site for residue GLY C 712
source : AE8
43) chain C
residue 454
type
sequence F
description binding site for residue GLY C 712
source : AE8
44) chain C
residue 450
type
sequence Y
description binding site for residue GLY C 713
source : AE9
45) chain C
residue 452
type
sequence N
description binding site for residue GLY C 713
source : AE9
46) chain C
residue 305
type
sequence R
description binding site for residue PO4 C 714
source : AF1
47) chain C
residue 348
type
sequence R
description binding site for residue PO4 C 714
source : AF1
48) chain C
residue 517
type
sequence H
description binding site for residue PO4 C 714
source : AF1
49) chain C
residue 531
type
sequence R
description binding site for residue PO4 C 714
source : AF1
50) chain C
residue 116
type
sequence K
description binding site for residue GTP B 703
source : AF4
51) chain C
residue 117
type
sequence V
description binding site for residue GTP B 703
source : AF4
52) chain C
residue 118
type
sequence I
description binding site for residue GTP B 703
source : AF4
53) chain C
residue 137
type
sequence D
description binding site for residue GTP B 703
source : AF4
54) chain C
residue 142
type
sequence Q
description binding site for residue GTP B 703
source : AF4
55) chain C
residue 145
type
sequence R
description binding site for residue GTP B 703
source : AF4
56) chain C
residue 165
type
sequence F
description binding site for residue GTP B 703
source : AF4
57) chain C
residue 425
type
sequence N
description binding site for residue NA B 706
source : AF7
58) chain C
residue 156
type
sequence V
description binding site for residue HDV A 702
source : AG4
59) chain C
residue 157
type
sequence F
description binding site for residue HDV A 702
source : AG4
60) chain C
residue 325
type
sequence I
description binding site for residue HDV A 702
source : AG4
61) chain C
residue 372
type
sequence R
description binding site for residue HDV A 702
source : AG4
62) chain C
residue 376
type
sequence H
description binding site for residue HDV A 702
source : AG4
63) chain C
residue 377
type
sequence K
description binding site for residue HDV A 702
source : AG4
64) chain C
residue 378
type
sequence V
description binding site for residue HDV A 702
source : AG4
65) chain C
residue 324
type
sequence G
description binding site for residue NA A 708
source : AH1
66) chain C
residue 371
type
sequence R
description binding site for residue GLY A 715
source : AH8
67) chain C
residue 372
type
sequence R
description binding site for residue GLY A 715
source : AH8
68) chain C
residue 233
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000305|PubMed:22056990
source Swiss-Prot : SWS_FT_FI1
69) chain C
residue 352
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
70) chain C
residue 358
type BINDING
sequence N
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
71) chain C
residue 523
type BINDING
sequence K
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
72) chain C
residue 116
type BINDING
sequence K
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
73) chain C
residue 137
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
74) chain C
residue 333
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI2
75) chain C
residue 455
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI3
76) chain C
residue 119
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI3
77) chain C
residue 376
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI3
78) chain C
residue 377
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI3
79) chain C
residue 451
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI3
80) chain C
residue 164
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
81) chain C
residue 210
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
82) chain C
residue 309
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
83) chain C
residue 315
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
84) chain C
residue 319
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
85) chain C
residue 366
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
86) chain C
residue 370
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
87) chain C
residue 149
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
88) chain C
residue 167
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI5
89) chain C
residue 206
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI5
90) chain C
residue 207
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI5
91) chain C
residue 311
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200
source Swiss-Prot : SWS_FT_FI5
92) chain C
residue 592
type MOD_RES
sequence T
description Phosphothreonine; by CDK1 => ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:29610582, ECO:0000269|PubMed:29670289, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6
93) chain C
residue 467
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI7
94) chain C
residue 469
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI7
95) chain C
residue 492
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI7

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