4Q7H
Crystal structure of SAMHD1 catalytic core with GTP
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 901 |
Chain | Residue |
A | HIS167 |
A | HIS206 |
A | ASP207 |
A | ASP311 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GTP A 902 |
Chain | Residue |
A | GLN142 |
A | ARG145 |
A | PHE165 |
B | TYR155 |
B | VAL156 |
B | VAL378 |
B | ARG451 |
B | HOH1002 |
A | VAL117 |
A | ILE118 |
A | VAL133 |
A | ILE136 |
A | ASP137 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 901 |
Chain | Residue |
B | ARG164 |
B | HIS167 |
B | HIS206 |
B | ASP207 |
B | ASP311 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GTP B 902 |
Chain | Residue |
A | TYR155 |
A | VAL156 |
A | VAL378 |
A | ARG451 |
A | LEU453 |
A | PHE454 |
A | LYS455 |
B | LYS116 |
B | VAL117 |
B | ILE118 |
B | VAL133 |
B | ASP137 |
B | GLN142 |
B | ARG145 |
B | PHE165 |
B | HOH1012 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 901 |
Chain | Residue |
C | HIS167 |
C | HIS206 |
C | ASP207 |
C | ASP311 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GTP C 902 |
Chain | Residue |
C | LYS116 |
C | VAL117 |
C | ILE118 |
C | ILE136 |
C | ASP137 |
C | GLN142 |
C | ARG145 |
C | PHE165 |
D | TYR155 |
D | VAL156 |
D | VAL378 |
D | ARG451 |
D | LEU453 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 901 |
Chain | Residue |
D | HIS167 |
D | HIS206 |
D | ASP207 |
D | ASP311 |
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 | 24 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | LYS116 | |
B | ARG352 | |
B | ASN358 | |
B | LYS523 | |
C | LYS116 | |
C | ASP137 | |
C | ARG333 | |
C | ARG352 | |
C | ASN358 | |
C | LYS523 | |
D | LYS116 | |
A | ASP137 | |
D | ASP137 | |
D | ARG333 | |
D | ARG352 | |
D | ASN358 | |
D | LYS523 | |
A | ARG333 | |
A | ARG352 | |
A | ASN358 | |
A | LYS523 | |
B | LYS116 | |
B | ASP137 | |
B | ARG333 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ASN119 | |
B | LYS455 | |
C | ASN119 | |
C | HIS376 | |
C | LYS377 | |
C | ARG451 | |
C | LYS455 | |
D | ASN119 | |
D | HIS376 | |
D | LYS377 | |
D | ARG451 | |
A | HIS376 | |
D | LYS455 | |
A | LYS377 | |
A | ARG451 | |
A | LYS455 | |
B | ASN119 | |
B | HIS376 | |
B | LYS377 | |
B | ARG451 |
site_id | SWS_FT_FI4 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24141705 |
Chain | Residue | Details |
A | GLN149 | |
B | ARG164 | |
B | HIS210 | |
B | ASP309 | |
B | TYR315 | |
B | ASP319 | |
B | ARG366 | |
B | HIS370 | |
C | GLN149 | |
C | ARG164 | |
C | HIS210 | |
A | ARG164 | |
C | ASP309 | |
C | TYR315 | |
C | ASP319 | |
C | ARG366 | |
C | HIS370 | |
D | GLN149 | |
D | ARG164 | |
D | HIS210 | |
D | ASP309 | |
D | TYR315 | |
A | HIS210 | |
D | ASP319 | |
D | ARG366 | |
D | HIS370 | |
A | ASP309 | |
A | TYR315 | |
A | ASP319 | |
A | ARG366 | |
A | HIS370 | |
B | GLN149 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200 |
Chain | Residue | Details |
A | HIS167 | |
C | HIS206 | |
C | ASP207 | |
C | ASP311 | |
D | HIS167 | |
D | HIS206 | |
D | ASP207 | |
D | ASP311 | |
A | HIS206 | |
A | ASP207 | |
A | ASP311 | |
B | HIS167 | |
B | HIS206 | |
B | ASP207 | |
B | ASP311 | |
C | HIS167 |
site_id | SWS_FT_FI6 |
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_FI7 |
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 |