4QMG
The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004518 | molecular_function | nuclease activity |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004518 | molecular_function | nuclease activity |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0004518 | molecular_function | nuclease activity |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0004518 | molecular_function | nuclease activity |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0004518 | molecular_function | nuclease activity |
F | 0043066 | biological_process | negative regulation of apoptotic process |
F | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
F | 0045766 | biological_process | positive regulation of angiogenesis |
G | 0043066 | biological_process | negative regulation of apoptotic process |
G | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
G | 0045766 | biological_process | positive regulation of angiogenesis |
H | 0043066 | biological_process | negative regulation of apoptotic process |
H | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
H | 0045766 | biological_process | positive regulation of angiogenesis |
I | 0043066 | biological_process | negative regulation of apoptotic process |
I | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
I | 0045766 | biological_process | positive regulation of angiogenesis |
J | 0043066 | biological_process | negative regulation of apoptotic process |
J | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
J | 0045766 | biological_process | positive regulation of angiogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | SER170 |
A | HIS171 |
A | ILE173 |
A | ASP175 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS A 402 |
Chain | Residue |
A | MSE163 |
A | SER165 |
A | GLY167 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 401 |
Chain | Residue |
B | ARG174 |
B | GLU200 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS B 402 |
Chain | Residue |
B | MSE163 |
B | SER165 |
B | GLY167 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 403 |
Chain | Residue |
B | HIS201 |
B | ARG203 |
B | ARG209 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | HIS201 |
B | VAL202 |
B | LYS249 |
B | GLU253 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 401 |
Chain | Residue |
C | ARG83 |
C | ARG174 |
C | GLU200 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS C 402 |
Chain | Residue |
C | MSE163 |
C | SER165 |
C | GLY167 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 401 |
Chain | Residue |
D | ARG83 |
D | ARG174 |
D | GLU200 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS D 402 |
Chain | Residue |
D | MSE163 |
D | SER165 |
D | GLY167 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 403 |
Chain | Residue |
D | HIS201 |
D | ARG203 |
D | ARG209 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 401 |
Chain | Residue |
E | LEU59 |
E | ALA60 |
E | ARG83 |
E | ARG174 |
E | GLU200 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS E 402 |
Chain | Residue |
E | MSE163 |
E | SER165 |
E | GLY167 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL E 403 |
Chain | Residue |
E | HIS201 |
E | ARG203 |
E | ARG209 |
Functional Information from PROSITE/UniProt
site_id | PS01284 |
Number of Residues | 11 |
Details | TNASE_2 Thermonuclease family signature 2. TPQGReYGmIY |
Chain | Residue | Details |
A | THR103-TYR113 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR103 | |
E | THR240 | |
A | THR240 | |
B | THR103 | |
B | THR240 | |
C | THR103 | |
C | THR240 | |
D | THR103 | |
D | THR240 | |
E | THR103 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS193 | |
B | LYS193 | |
C | LYS193 | |
D | LYS193 | |
E | LYS193 |