3TY3
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
A | 0046872 | molecular_function | metal ion binding |
A | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
A | 0051287 | molecular_function | NAD binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
B | 0046872 | molecular_function | metal ion binding |
B | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GGG A 363 |
Chain | Residue |
A | GLY77 |
A | HOH454 |
A | HOH477 |
A | HOH487 |
A | HOH537 |
A | ALA78 |
A | VAL79 |
A | SER81 |
A | ILE93 |
A | ARG97 |
A | GLU285 |
A | PRO286 |
A | HIS288 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 364 |
Chain | Residue |
A | ILE17 |
A | ALA300 |
A | ASN301 |
A | ASP342 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 3968 |
Chain | Residue |
A | ASP44 |
A | LEU45 |
A | ASP46 |
A | ARG62 |
A | THR63 |
A | ARG66 |
A | HOH502 |
A | HOH535 |
B | ARG27 |
B | ASN350 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 3969 |
Chain | Residue |
A | HIS186 |
A | LYS188 |
A | CYS244 |
A | HOH412 |
A | HOH591 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GGG B 363 |
Chain | Residue |
B | GLY77 |
B | ALA78 |
B | VAL79 |
B | SER81 |
B | ILE93 |
B | ARG97 |
B | GLU285 |
B | PRO286 |
B | VAL287 |
B | HIS288 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 364 |
Chain | Residue |
B | LYS110 |
B | ASP121 |
B | ARG174 |
B | ILE177 |
B | ARG178 |
B | SER184 |
Functional Information from PROSITE/UniProt
site_id | PS00470 |
Number of Residues | 20 |
Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDgaAsli.GSLGL |
Chain | Residue | Details |
A | ASN252-LEU271 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q72IW9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"Q72IW9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18257517","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |