2CZC
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii OT3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006096 | biological_process | glycolytic process |
A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
A | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006096 | biological_process | glycolytic process |
B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
B | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006096 | biological_process | glycolytic process |
C | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
C | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006096 | biological_process | glycolytic process |
D | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
D | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 601 |
Chain | Residue |
A | SER140 |
A | CYS141 |
A | ASN142 |
A | ARG166 |
A | HIS191 |
A | HIS192 |
A | HOH644 |
A | HOH746 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 602 |
Chain | Residue |
A | ARG167 |
A | ALA168 |
A | ARG176 |
A | HOH737 |
A | ARG166 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 603 |
Chain | Residue |
B | SER140 |
B | CYS141 |
B | ASN142 |
B | ARG166 |
B | HIS191 |
B | HIS192 |
B | HOH691 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 C 604 |
Chain | Residue |
C | SER140 |
C | CYS141 |
C | ASN142 |
C | ARG166 |
C | HIS191 |
C | HIS192 |
C | HOH679 |
C | HOH681 |
C | HOH703 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 D 605 |
Chain | Residue |
D | SER140 |
D | CYS141 |
D | ASN142 |
D | HIS191 |
D | HIS192 |
D | HOH653 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD A 501 |
Chain | Residue |
A | ASN8 |
A | TYR10 |
A | GLY11 |
A | THR12 |
A | ILE13 |
A | THR35 |
A | ALA54 |
A | ALA86 |
A | THR87 |
A | PRO88 |
A | GLN109 |
A | GLY111 |
A | CYS141 |
A | ARG167 |
A | ASP170 |
A | GLN298 |
A | HOH614 |
A | HOH621 |
A | HOH625 |
A | HOH682 |
A | HOH747 |
A | HOH749 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD B 502 |
Chain | Residue |
B | ASN8 |
B | GLY9 |
B | TYR10 |
B | GLY11 |
B | THR12 |
B | ILE13 |
B | THR35 |
B | ALA54 |
B | ALA86 |
B | THR87 |
B | PRO88 |
B | GLN109 |
B | GLY111 |
B | CYS141 |
B | ARG167 |
B | ASP170 |
B | GLN298 |
B | HOH617 |
B | HOH640 |
B | HOH650 |
B | HOH672 |
B | HOH726 |
B | HOH728 |
site_id | AC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD C 503 |
Chain | Residue |
C | HOH715 |
C | HOH716 |
C | ASN8 |
C | GLY9 |
C | TYR10 |
C | GLY11 |
C | THR12 |
C | ILE13 |
C | ALA86 |
C | THR87 |
C | GLN109 |
C | GLY111 |
C | CYS141 |
C | ARG167 |
C | ASP170 |
C | GLN298 |
C | HOH613 |
C | HOH643 |
C | HOH679 |
C | HOH710 |
C | HOH714 |
site_id | AC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD D 504 |
Chain | Residue |
D | ASN8 |
D | TYR10 |
D | GLY11 |
D | THR12 |
D | ILE13 |
D | ALA54 |
D | ALA86 |
D | THR87 |
D | PRO88 |
D | GLY89 |
D | GLN109 |
D | GLY111 |
D | CYS141 |
D | ARG167 |
D | ASP170 |
D | GLN298 |
D | HOH610 |
D | HOH642 |
D | HOH675 |
D | HOH695 |
D | HOH696 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. VSCNTTgL |
Chain | Residue | Details |
A | VAL139-LEU146 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | CYS141 | |
B | CYS141 | |
C | CYS141 | |
D | CYS141 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | THR12 | |
C | GLY111 | |
C | ARG167 | |
C | GLN298 | |
D | THR12 | |
D | GLY111 | |
D | ARG167 | |
D | GLN298 | |
A | GLY111 | |
A | ARG167 | |
A | GLN298 | |
B | THR12 | |
B | GLY111 | |
B | ARG167 | |
B | GLN298 | |
C | THR12 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER140 | |
A | HIS192 | |
B | SER140 | |
B | HIS192 | |
C | SER140 | |
C | HIS192 | |
D | SER140 | |
D | HIS192 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cf2 |
Chain | Residue | Details |
A | CYS141 | |
A | HIS217 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cf2 |
Chain | Residue | Details |
B | CYS141 | |
B | HIS217 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cf2 |
Chain | Residue | Details |
C | CYS141 | |
C | HIS217 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cf2 |
Chain | Residue | Details |
D | CYS141 | |
D | HIS217 |