6KEZ
Crystal structure of GAPDH/CP12/PRK complex from Arabidopsis thaliana
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006006 | biological_process | glucose metabolic process |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0006006 | biological_process | glucose metabolic process |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0006006 | biological_process | glucose metabolic process |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0006006 | biological_process | glucose metabolic process |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
E | 0006006 | biological_process | glucose metabolic process |
E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
E | 0050661 | molecular_function | NADP binding |
E | 0051287 | molecular_function | NAD binding |
F | 0006006 | biological_process | glucose metabolic process |
F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
F | 0050661 | molecular_function | NADP binding |
F | 0051287 | molecular_function | NAD binding |
G | 0006006 | biological_process | glucose metabolic process |
G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
G | 0050661 | molecular_function | NADP binding |
G | 0051287 | molecular_function | NAD binding |
H | 0006006 | biological_process | glucose metabolic process |
H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
H | 0050661 | molecular_function | NADP binding |
H | 0051287 | molecular_function | NAD binding |
I | 0005524 | molecular_function | ATP binding |
I | 0005975 | biological_process | carbohydrate metabolic process |
I | 0008974 | molecular_function | phosphoribulokinase activity |
I | 0016301 | molecular_function | kinase activity |
J | 0005524 | molecular_function | ATP binding |
J | 0005975 | biological_process | carbohydrate metabolic process |
J | 0008974 | molecular_function | phosphoribulokinase activity |
J | 0016301 | molecular_function | kinase activity |
K | 0005524 | molecular_function | ATP binding |
K | 0005975 | biological_process | carbohydrate metabolic process |
K | 0008974 | molecular_function | phosphoribulokinase activity |
K | 0016301 | molecular_function | kinase activity |
L | 0005524 | molecular_function | ATP binding |
L | 0005975 | biological_process | carbohydrate metabolic process |
L | 0008974 | molecular_function | phosphoribulokinase activity |
L | 0016301 | molecular_function | kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | ASN7 |
A | GLY98 |
A | THR99 |
A | GLY100 |
A | THR122 |
A | CYS153 |
A | ASN316 |
A | GLU317 |
A | TYR320 |
P | GLU69 |
P | TYR76 |
A | PHE9 |
P | ASN78 |
A | GLY10 |
A | ARG11 |
A | ILE12 |
A | ASN34 |
A | ASP35 |
A | THR36 |
A | ARG80 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | PHE9 |
B | GLY10 |
B | ARG11 |
B | ILE12 |
B | ASP35 |
B | THR36 |
B | ARG80 |
B | GLY98 |
B | GLY100 |
B | THR122 |
B | ALA123 |
B | CYS153 |
B | ASN316 |
B | TYR320 |
G | PHE254 |
site_id | AC3 |
Number of Residues | 18 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | PHE9 |
C | GLY10 |
C | ARG11 |
C | ILE12 |
C | ASP35 |
C | THR36 |
C | GLY98 |
C | THR99 |
C | GLY100 |
C | ALA123 |
C | CYS153 |
C | THR183 |
C | ASN316 |
C | GLU317 |
C | TYR320 |
O | GLU69 |
O | TYR76 |
O | ASN78 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue NAD D 401 |
Chain | Residue |
A | SER192 |
D | ASN7 |
D | GLY10 |
D | ARG11 |
D | ILE12 |
D | ASP35 |
D | THR36 |
D | ARG80 |
D | GLY100 |
D | THR122 |
D | ALA123 |
D | SER152 |
D | ASN316 |
D | TYR320 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue NAD E 401 |
Chain | Residue |
E | ASN7 |
E | ARG11 |
E | ILE12 |
E | ASP35 |
E | THR36 |
E | ARG80 |
E | THR99 |
E | GLY100 |
E | THR122 |
E | ALA123 |
E | CYS153 |
E | THR183 |
E | ASN316 |
E | TYR320 |
E | HOH502 |
H | SER192 |
site_id | AC6 |
Number of Residues | 17 |
Details | binding site for residue NAD F 401 |
Chain | Residue |
N | ASN78 |
F | ASN7 |
F | GLY10 |
F | ARG11 |
F | ILE12 |
F | ASN34 |
F | ASP35 |
F | THR36 |
F | GLY98 |
F | THR99 |
F | GLY100 |
F | THR122 |
F | CYS153 |
F | THR183 |
F | ASN316 |
F | TYR320 |
N | TYR76 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue NAD G 401 |
Chain | Residue |
B | PHE254 |
G | ASN7 |
G | GLY10 |
G | ARG11 |
G | ILE12 |
G | ASP35 |
G | ARG80 |
G | GLY98 |
G | GLY100 |
G | THR122 |
G | ALA123 |
G | CYS153 |
G | HIS180 |
G | THR183 |
G | ASN316 |
G | TYR320 |
site_id | AC8 |
Number of Residues | 19 |
Details | binding site for residue NAD H 401 |
Chain | Residue |
H | ASN7 |
H | GLY10 |
H | ARG11 |
H | ILE12 |
H | ASN34 |
H | ASP35 |
H | THR36 |
H | ARG80 |
H | GLY98 |
H | THR99 |
H | GLY100 |
H | THR122 |
H | ALA123 |
H | CYS153 |
H | ASN316 |
H | GLU317 |
M | GLU69 |
M | TYR76 |
M | ASN78 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20516587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22514274","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 136 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 104 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |