7MDH
STRUCTURAL BASIS FOR LIGHT ACITVATION OF A CHLOROPLAST ENZYME. THE STRUCTURE OF SORGHUM NADP-MALATE DEHYDROGENASE IN ITS OXIDIZED FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016615 | molecular_function | malate dehydrogenase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016615 | molecular_function | malate dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006108 | biological_process | malate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016615 | molecular_function | malate dehydrogenase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006108 | biological_process | malate metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016615 | molecular_function | malate dehydrogenase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | ASN173 |
| A | CYS175 |
| A | LEU197 |
| A | HIS229 |
| A | HOH525 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | GLU320 |
| A | ASP321 |
| A | LYS363 |
| A | GLU372 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | ASP201 |
| A | HIS229 |
| A | LEU385 |
| A | HOH524 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 504 |
| Chain | Residue |
| A | ASP23 |
| A | GLU118 |
| A | GLU121 |
| D | GLU86 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | GLU109 |
| B | HOH512 |
| D | ASP346 |
| D | GLU350 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | ASP122 |
| B | HOH516 |
| B | HOH517 |
| D | THR254 |
| D | GLU258 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 503 |
| Chain | Residue |
| B | ASP201 |
| B | HIS229 |
| B | LEU385 |
| B | HOH543 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 504 |
| Chain | Residue |
| B | ASN173 |
| B | CYS175 |
| B | HIS229 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 505 |
| Chain | Residue |
| B | THR254 |
| B | GLU258 |
| D | ASP122 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| B | HIS368 |
| B | HOH558 |
| C | GLU93 |
| D | LYS275 |
| D | HOH586 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 502 |
| Chain | Residue |
| C | GLU320 |
| C | ASP321 |
| C | LYS363 |
| C | GLU372 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN C 503 |
| Chain | Residue |
| C | ASP201 |
| C | HIS229 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 504 |
| Chain | Residue |
| C | ASN173 |
| C | CYS175 |
| C | HIS229 |
| C | HOH523 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| A | GLU93 |
| D | ASP145 |
| D | HIS368 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 502 |
| Chain | Residue |
| D | ASP201 |
| D | HIS229 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 503 |
| Chain | Residue |
| B | ASP346 |
| B | GLU350 |
| D | GLU109 |
| D | HOH568 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN C 505 |
| Chain | Residue |
| C | LYS275 |
| D | GLU93 |
| site_id | CAA |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | ASP201 |
| A | HIS229 |
| site_id | CAB |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| B | ASP201 |
| B | HIS229 |
| site_id | CAC |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| C | ASP201 |
| C | HIS229 |
| site_id | CAD |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| D | ASP201 |
| D | HIS229 |
| site_id | CSA |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | CYS365 |
| A | CYS377 |
| site_id | CSB |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| B | CYS365 |
| B | CYS377 |
| site_id | CSC |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| C | CYS365 |
| C | CYS377 |
| site_id | CSD |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| D | CYS365 |
| D | CYS377 |
| site_id | NSA |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | CYS29 |
| A | CYS24 |
| site_id | NSB |
| Number of Residues | 2 |
| Details | N-TERMINAL REDOX-REGULATED DISULFIDE |
| Chain | Residue |
| B | CYS24 |
| B | CYS29 |
| site_id | NSC |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| C | CYS24 |
| C | CYS29 |
| site_id | NSD |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| D | CYS24 |
| D | CYS29 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. LTRLDenRAkcqL |
| Chain | Residue | Details |
| A | LEU197-LEU209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10004","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Activation of NADP-MDH"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ASP201 | |
| A | ASN228 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASP201 | |
| B | ASN228 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ASP201 | |
| C | ASN228 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ASP201 | |
| D | ASN228 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ARG204 | |
| A | HIS229 | |
| A | ASP201 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ARG204 | |
| B | HIS229 | |
| B | ASP201 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ARG204 | |
| C | HIS229 | |
| C | ASP201 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ARG204 | |
| D | HIS229 | |
| D | ASP201 |
