eF-site ID 6cm2-C
PDB Code 6cm2
Chain C

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Title SAMHD1 HD domain bound to decitabine triphosphate
Classification HYDROLASE
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 F6G D 703
source : AC3
2) chain C
residue 118
type
sequence I
description binding site for residue F6G D 703
source : AC3
3) chain C
residue 119
type
sequence N
description binding site for residue F6G D 703
source : AC3
4) chain C
residue 149
type
sequence Q
description binding site for residue F6G C 701
source : AC4
5) chain C
residue 150
type
sequence L
description binding site for residue F6G C 701
source : AC4
6) chain C
residue 164
type
sequence R
description binding site for residue F6G C 701
source : AC4
7) chain C
residue 206
type
sequence R
description binding site for residue F6G C 701
source : AC4
8) chain C
residue 215
type
sequence H
description binding site for residue F6G C 701
source : AC4
9) chain C
residue 233
type
sequence H
description binding site for residue F6G C 701
source : AC4
10) chain C
residue 312
type
sequence K
description binding site for residue F6G C 701
source : AC4
11) chain C
residue 315
type
sequence Y
description binding site for residue F6G C 701
source : AC4
12) chain C
residue 319
type
sequence D
description binding site for residue F6G C 701
source : AC4
13) chain C
residue 366
type
sequence R
description binding site for residue F6G C 701
source : AC4
14) chain C
residue 370
type
sequence H
description binding site for residue F6G C 701
source : AC4
15) chain C
residue 374
type
sequence Y
description binding site for residue F6G C 701
source : AC4
16) chain C
residue 375
type
sequence Q
description binding site for residue F6G C 701
source : AC4
17) chain C
residue 116
type
sequence K
description binding site for residue MG C 702
source : AC5
18) chain C
residue 333
type
sequence R
description binding site for residue F6G C 703
source : AC6
19) chain C
residue 337
type
sequence F
description binding site for residue F6G C 703
source : AC6
20) chain C
residue 352
type
sequence R
description binding site for residue F6G C 703
source : AC6
21) chain C
residue 354
type
sequence K
description binding site for residue F6G C 703
source : AC6
22) chain C
residue 523
type
sequence K
description binding site for residue F6G C 703
source : AC6
23) chain C
residue 155
type
sequence Y
description binding site for residue GTP B 703
source : AD1
24) chain C
residue 156
type
sequence V
description binding site for residue GTP B 703
source : AD1
25) chain C
residue 451
type
sequence R
description binding site for residue GTP B 703
source : AD1
26) chain C
residue 455
type
sequence K
description binding site for residue GTP B 703
source : AD1
27) chain C
residue 116
type
sequence K
description binding site for residue GTP B 705
source : AD3
28) chain C
residue 117
type
sequence V
description binding site for residue GTP B 705
source : AD3
29) chain C
residue 118
type
sequence I
description binding site for residue GTP B 705
source : AD3
30) chain C
residue 137
type
sequence D
description binding site for residue GTP B 705
source : AD3
31) chain C
residue 142
type
sequence Q
description binding site for residue GTP B 705
source : AD3
32) chain C
residue 145
type
sequence R
description binding site for residue GTP B 705
source : AD3
33) chain C
residue 165
type
sequence F
description binding site for residue GTP B 705
source : AD3
34) chain C
residue 156
type
sequence V
description binding site for residue F6G A 701
source : AD4
35) chain C
residue 157
type
sequence F
description binding site for residue F6G A 701
source : AD4
36) chain C
residue 372
type
sequence R
description binding site for residue F6G A 701
source : AD4
37) chain C
residue 376
type
sequence H
description binding site for residue F6G A 701
source : AD4
38) chain C
residue 377
type
sequence K
description binding site for residue F6G A 701
source : AD4
39) chain C
residue 378
type
sequence V
description binding site for residue F6G A 701
source : AD4
40) chain C
residue 523
type
sequence K
description binding site for residue GTP A 704
source : AD7
41) 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
42) 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
43) 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
44) chain C
residue 233
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000305|PubMed:22056990
source Swiss-Prot : SWS_FT_FI1
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) chain C
residue 164
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
57) chain C
residue 210
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
58) chain C
residue 309
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
59) chain C
residue 315
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
60) chain C
residue 319
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
61) chain C
residue 366
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
62) chain C
residue 370
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
63) chain C
residue 149
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:24141705
source Swiss-Prot : SWS_FT_FI4
64) 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
65) 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
66) 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
67) 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
68) 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

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