1TEH
STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001523 | biological_process | retinoid metabolic process |
A | 0003016 | biological_process | respiratory system process |
A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009055 | molecular_function | electron transfer activity |
A | 0010430 | biological_process | fatty acid omega-oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
A | 0032496 | biological_process | response to lipopolysaccharide |
A | 0042802 | molecular_function | identical protein binding |
A | 0044281 | biological_process | small molecule metabolic process |
A | 0045777 | biological_process | positive regulation of blood pressure |
A | 0046294 | biological_process | formaldehyde catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051409 | biological_process | response to nitrosative stress |
A | 0051775 | biological_process | response to redox state |
A | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) activity |
A | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
A | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
B | 0001523 | biological_process | retinoid metabolic process |
B | 0003016 | biological_process | respiratory system process |
B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005829 | cellular_component | cytosol |
B | 0006629 | biological_process | lipid metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009055 | molecular_function | electron transfer activity |
B | 0010430 | biological_process | fatty acid omega-oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
B | 0032496 | biological_process | response to lipopolysaccharide |
B | 0042802 | molecular_function | identical protein binding |
B | 0044281 | biological_process | small molecule metabolic process |
B | 0045777 | biological_process | positive regulation of blood pressure |
B | 0046294 | biological_process | formaldehyde catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051409 | biological_process | response to nitrosative stress |
B | 0051775 | biological_process | response to redox state |
B | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
B | 0070062 | cellular_component | extracellular exosome |
B | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) activity |
B | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
B | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 375 |
Chain | Residue |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | CYS111 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 376 |
Chain | Residue |
A | CYS46 |
A | HIS67 |
A | GLU68 |
A | CYS174 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 375 |
Chain | Residue |
B | CYS97 |
B | GLY98 |
B | CYS100 |
B | CYS103 |
B | CYS111 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 376 |
Chain | Residue |
B | CYS46 |
B | HIS67 |
B | GLU68 |
B | CYS174 |
B | ARG369 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 378 |
Chain | Residue |
B | GLU360 |
B | GLU360 |
B | HIS363 |
B | HIS363 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD A 377 |
Chain | Residue |
A | HIS47 |
A | TYR93 |
A | THR178 |
A | GLY202 |
A | VAL203 |
A | ASP223 |
A | ILE224 |
A | CYS268 |
A | ILE269 |
A | VAL274 |
A | VAL292 |
A | GLY293 |
A | VAL294 |
A | THR317 |
A | ALA318 |
A | PHE319 |
A | ARG369 |
A | HOH382 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD B 377 |
Chain | Residue |
B | HIS47 |
B | THR178 |
B | LEU200 |
B | GLY201 |
B | GLY202 |
B | VAL203 |
B | ASP223 |
B | ILE224 |
B | LYS228 |
B | CYS268 |
B | ILE269 |
B | VAL274 |
B | VAL292 |
B | GLY293 |
B | VAL294 |
B | THR317 |
B | PHE319 |
B | ARG369 |
site_id | ZN1 |
Number of Residues | 5 |
Details | ZNA1 IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. |
Chain | Residue |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | CYS111 |
A | ZN375 |
site_id | ZN2 |
Number of Residues | 6 |
Details | GLU 68 IS NEARLY-COORDINATED TO THE ZINC, 2.87 ANGSTROMS. HOH A401 IS 3.18 ANGSTROMS TO THE ZINC. ZNB IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. ZNB IS SET TO BOND TO CYS 46, HIS 67 AND CYS 174 IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. |
Chain | Residue |
A | HOH378 |
A | ZN376 |
A | CYS46 |
A | HIS67 |
A | GLU68 |
A | CYS174 |
site_id | ZN3 |
Number of Residues | 5 |
Details | ZNB1 IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. |
Chain | Residue |
B | CYS97 |
B | CYS100 |
B | CYS103 |
B | CYS111 |
B | ZN375 |
site_id | ZN4 |
Number of Residues | 5 |
Details | GLU 68 IS COORDINATED TO THE ZINC, 2.04 ANGSTROMS. ZNB IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. ZNB IS SET TO BOND TO CYS 46, HIS 67 AND CYS 174 IN CHITOPH19.ZNC AND CHIPARAM1.ZNC. |
Chain | Residue |
B | CYS46 |
B | HIS67 |
B | GLU68 |
B | CYS174 |
B | ZN376 |
site_id | ZNS |
Number of Residues | 3 |
Details | THIS ZINC IS POSITIONED ON CRYSTALLOGRAPHIC X AXIS, THEREFORE ASSIGNED AN OCCUPANCY OF 0.5 IN ORDER TO BE REFINED AS SPECIAL POSITION ATOM IN XPLOR. THE OTHER TWO LIGANDS ARE HIS 360 AND GLU 363 FROM THE SYMMETRY COPIES. ZNS IS DEFINED IN CHITOPH19.ZNS AND CHIPARAM19.ZNS. IT IS NOT PRESET TO BOND WITH HIS AND GLU. |
Chain | Residue |
B | GLU360 |
B | HIS363 |
B | ZN378 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgAGIvesvGegV |
Chain | Residue | Details |
A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:3365377 |
Chain | Residue | Details |
A | HIS47 | |
B | GLY98 | |
B | LYS101 | |
B | LEU104 | |
B | GLN112 | |
B | GLY175 | |
A | GLU68 | |
A | GLY98 | |
A | LYS101 | |
A | LEU104 | |
A | GLN112 | |
A | GLY175 | |
B | HIS47 | |
B | GLU68 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Important for FDH activity and activation by fatty acids => ECO:0000269|PubMed:8460164, ECO:0000269|PubMed:8494891 |
Chain | Residue | Details |
A | VAL116 | |
B | VAL116 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ASN4 | |
B | ASN4 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P28474 |
Chain | Residue | Details |
A | GLU234 | |
A | GLY316 | |
B | GLU234 | |
B | GLY316 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | LYS248 | |
B | LYS248 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | VAL325 | |
A | PHE352 | |
B | VAL325 | |
B | PHE352 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 12196016, 12484756 |
Chain | Residue | Details |
A | THR48 | |
A | HIS47 |
site_id | CSA2 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 12196016, 12484756 |
Chain | Residue | Details |
B | THR48 | |
B | HIS47 |
site_id | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 464 |
Chain | Residue | Details |
A | HIS47 | metal ligand |
A | VAL116 | activator |
A | GLY175 | metal ligand |
A | THR370 | steric role |
A | THR48 | proton shuttle (general acid/base) |
A | ASP49 | proton shuttle (general acid/base) |
A | GLU68 | metal ligand |
A | GLY69 | metal ligand |
A | GLY98 | metal ligand |
A | LYS101 | metal ligand |
A | LEU104 | metal ligand |
A | GLN112 | metal ligand |
site_id | MCSA2 |
Number of Residues | 12 |
Details | M-CSA 464 |
Chain | Residue | Details |
B | HIS47 | metal ligand |
B | VAL116 | activator |
B | GLY175 | metal ligand |
B | THR370 | steric role |
B | THR48 | proton shuttle (general acid/base) |
B | ASP49 | proton shuttle (general acid/base) |
B | GLU68 | metal ligand |
B | GLY69 | metal ligand |
B | GLY98 | metal ligand |
B | LYS101 | metal ligand |
B | LEU104 | metal ligand |
B | GLN112 | metal ligand |