9EC2

Crystal structure of SAMHD1 dimer bound to an inhibitor obtained from high-throughput chemical tethering to the guanine antiviral acyclovir

This is a non-PDB format compatible entry.

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:22056990

Chain	Residue	Details
A	HIS233
B	HIS233
C	HIS233
D	HIS233

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: in chain B => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNP, ECO:0007744|PDB:4TNQ, ECO:0007744|PDB:4TNR, ECO:0007744|PDB:4TNX

Chain	Residue	Details
A	LYS116
B	ARG145
C	LYS116
C	VAL117
C	ASP137
C	GLN142
C	ARG145
D	LYS116
D	VAL117
D	ASP137
D	GLN142
A	VAL117
D	ARG145
A	ASP137
A	GLN142
A	ARG145
B	LYS116
B	VAL117
B	ASP137
B	GLN142

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: in chain B => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNQ

Chain	Residue	Details
A	ASN119
B	ASN119
C	ASN119
D	ASN119

---

site_id	SWS_FT_FI4
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNQ

Chain	Residue	Details
A	GLN149
B	ARG164
B	HIS210
B	HIS215
B	LYS312
B	TYR315
B	ASP319
B	GLN375
C	GLN149
C	ARG164
C	HIS210
A	ARG164
C	HIS215
C	LYS312
C	TYR315
C	ASP319
C	GLN375
D	GLN149
D	ARG164
D	HIS210
D	HIS215
D	LYS312
A	HIS210
D	TYR315
D	ASP319
D	GLN375
A	HIS215
A	LYS312
A	TYR315
A	ASP319
A	GLN375
B	GLN149

---

site_id	SWS_FT_FI5
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:24141705, ECO:0007744|PDB:4BZB

Chain	Residue	Details
A	LEU150
B	HIS206
B	ASP207
B	ASP311
B	ARG366
B	TYR374
C	LEU150
C	HIS167
C	HIS206
C	ASP207
C	ASP311
A	HIS167
C	ARG366
C	TYR374
D	LEU150
D	HIS167
D	HIS206
D	ASP207
D	ASP311
D	ARG366
D	TYR374
A	HIS206
A	ASP207
A	ASP311
A	ARG366
A	TYR374
B	LEU150
B	HIS167

---

site_id	SWS_FT_FI6
Number of Residues	16
Details	BINDING: in chain C => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNQ

Chain	Residue	Details
A	VAL156
C	ARG372
C	HIS376
C	LYS377
D	VAL156
D	ARG372
D	HIS376
D	LYS377
A	ARG372
A	HIS376
A	LYS377
B	VAL156
B	ARG372
B	HIS376
B	LYS377
C	VAL156

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	BINDING: in chain A => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNQ

Chain	Residue	Details
A	ARG333
D	ARG333
D	ARG352
D	LYS354
A	ARG352
A	LYS354
B	ARG333
B	ARG352
B	LYS354
C	ARG333
C	ARG352
C	LYS354

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: in chain A => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4BZB, ECO:0007744|PDB:4TNX

Chain	Residue	Details
A	ASN358
B	ASN358
C	ASN358
D	ASN358

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	BINDING: in chain C => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNP, ECO:0007744|PDB:4TNQ, ECO:0007744|PDB:4TNR, ECO:0007744|PDB:4TNX

Chain	Residue	Details
A	ARG451
A	LYS455
B	ARG451
B	LYS455
C	ARG451
C	LYS455
D	ARG451
D	LYS455

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	BINDING: in chain A => ECO:0000269|PubMed:25267621, ECO:0007744|PDB:4TNP, ECO:0007744|PDB:4TNQ, ECO:0007744|PDB:4TNR, ECO:0007744|PDB:4TNX

Chain	Residue	Details
A	LYS523
B	LYS523
C	LYS523
D	LYS523

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: 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

Chain	Residue	Details
A	THR592
B	THR592
C	THR592
D	THR592

---

site_id	SWS_FT_FI12
Number of Residues	20
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS467
B	LYS622
C	LYS467
C	LYS469
C	LYS492
C	LYS622
D	LYS467
D	LYS469
D	LYS492
D	LYS622
A	LYS469
A	LYS492
A	LYS622
B	LYS467
B	LYS469
B	LYS492

---