4ZCC
Renalase in complex with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| C | 0051287 | molecular_function | NAD binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| D | 0051287 | molecular_function | NAD binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | ILE8 |
| A | ARG40 |
| A | GLY54 |
| A | ALA55 |
| A | GLN56 |
| A | TYR57 |
| A | CYS126 |
| A | ILE128 |
| A | ALA157 |
| A | THR158 |
| A | PRO159 |
| A | GLY9 |
| A | GLN162 |
| A | HIS232 |
| A | ALA279 |
| A | GLY301 |
| A | ASP302 |
| A | ARG308 |
| A | VAL309 |
| A | ALA312 |
| A | NAI402 |
| A | HOH526 |
| A | GLY11 |
| A | HOH528 |
| A | HOH531 |
| A | HOH564 |
| A | HOH577 |
| A | HOH580 |
| A | HOH582 |
| A | HOH583 |
| A | ILE12 |
| A | ALA13 |
| A | ASP32 |
| A | LYS33 |
| A | SER34 |
| A | GLY39 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue NAI A 402 |
| Chain | Residue |
| A | TYR57 |
| A | THR59 |
| A | ARG61 |
| A | ASN87 |
| A | SER96 |
| A | ASP98 |
| A | GLN100 |
| A | ARG102 |
| A | THR185 |
| A | PHE204 |
| A | ALA279 |
| A | ARG280 |
| A | GLY307 |
| A | ARG308 |
| A | FAD401 |
| A | HOH501 |
| A | HOH510 |
| A | HOH531 |
| A | HOH535 |
| A | HOH560 |
| A | HOH612 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue FMT A 403 |
| Chain | Residue |
| A | SER37 |
| A | GLY38 |
| A | SER43 |
| A | LYS44 |
| A | SER110 |
| A | THR113 |
| A | ARG114 |
| A | HOH540 |
| site_id | AC4 |
| Number of Residues | 37 |
| Details | binding site for residue FAD B 401 |
| Chain | Residue |
| B | HOH574 |
| B | HOH577 |
| B | HOH609 |
| B | GLY9 |
| B | GLY11 |
| B | ILE12 |
| B | ALA13 |
| B | ASP32 |
| B | LYS33 |
| B | SER34 |
| B | GLY39 |
| B | ARG40 |
| B | GLY54 |
| B | ALA55 |
| B | GLN56 |
| B | TYR57 |
| B | CYS126 |
| B | ILE128 |
| B | ALA157 |
| B | THR158 |
| B | PRO159 |
| B | GLN162 |
| B | HIS232 |
| B | TRP276 |
| B | ALA279 |
| B | GLY301 |
| B | ASP302 |
| B | ARG308 |
| B | VAL309 |
| B | ALA312 |
| B | NAI402 |
| B | HOH510 |
| B | HOH521 |
| B | HOH538 |
| B | HOH546 |
| B | HOH572 |
| B | HOH573 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue NAI B 402 |
| Chain | Residue |
| B | TYR57 |
| B | THR59 |
| B | ARG61 |
| B | SER96 |
| B | ASP98 |
| B | ARG102 |
| B | THR185 |
| B | PHE204 |
| B | ALA279 |
| B | ARG280 |
| B | GLY307 |
| B | ARG308 |
| B | FAD401 |
| B | HOH521 |
| B | HOH524 |
| B | HOH536 |
| B | HOH558 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue FMT B 403 |
| Chain | Residue |
| B | SER37 |
| B | GLY38 |
| B | SER43 |
| B | LYS44 |
| B | SER110 |
| B | THR113 |
| B | ARG114 |
| B | HOH590 |
| site_id | AC7 |
| Number of Residues | 38 |
| Details | binding site for residue FAD C 401 |
| Chain | Residue |
| C | GLY9 |
| C | GLY11 |
| C | ILE12 |
| C | ALA13 |
| C | ASP32 |
| C | LYS33 |
| C | SER34 |
| C | GLY38 |
| C | GLY39 |
| C | ARG40 |
| C | MET41 |
| C | GLY54 |
| C | ALA55 |
| C | GLN56 |
| C | TYR57 |
| C | CYS126 |
| C | ILE128 |
| C | ALA157 |
| C | THR158 |
| C | PRO159 |
| C | GLN162 |
| C | HIS232 |
| C | TRP276 |
| C | ALA279 |
| C | GLY301 |
| C | ASP302 |
| C | GLY307 |
| C | ARG308 |
| C | VAL309 |
| C | ALA312 |
| C | NAI402 |
| C | HOH514 |
| C | HOH529 |
| C | HOH533 |
| C | HOH554 |
| C | HOH556 |
| C | HOH565 |
| C | HOH582 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue NAI C 402 |
| Chain | Residue |
| C | TYR57 |
| C | THR59 |
| C | ARG61 |
| C | ASN87 |
| C | SER96 |
| C | ASP98 |
| C | ARG102 |
| C | THR185 |
| C | PHE204 |
| C | ASP211 |
| C | HIS232 |
| C | ALA233 |
| C | ARG280 |
| C | ARG308 |
| C | FAD401 |
| C | HOH503 |
| C | HOH514 |
| C | HOH574 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue FMT C 403 |
| Chain | Residue |
| C | SER37 |
| C | GLY38 |
| C | SER110 |
| C | THR113 |
| C | ARG114 |
| C | HOH532 |
| site_id | AD1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD D 401 |
| Chain | Residue |
| D | GLY9 |
| D | GLY11 |
| D | ILE12 |
| D | ALA13 |
| D | ASP32 |
| D | LYS33 |
| D | SER34 |
| D | GLY39 |
| D | ARG40 |
| D | MET41 |
| D | GLY54 |
| D | ALA55 |
| D | GLN56 |
| D | TYR57 |
| D | CYS126 |
| D | ILE128 |
| D | ALA157 |
| D | THR158 |
| D | PRO159 |
| D | HIS232 |
| D | TRP276 |
| D | ALA279 |
| D | GLY301 |
| D | ASP302 |
| D | GLY307 |
| D | ARG308 |
| D | VAL309 |
| D | ALA312 |
| D | NAI402 |
| D | HOH520 |
| D | HOH541 |
| D | HOH548 |
| D | HOH553 |
| D | HOH557 |
| D | HOH568 |
| D | HOH569 |
| D | HOH601 |
| site_id | AD2 |
| Number of Residues | 18 |
| Details | binding site for residue NAI D 402 |
| Chain | Residue |
| D | TYR57 |
| D | THR59 |
| D | ARG61 |
| D | ASN87 |
| D | SER96 |
| D | ASP98 |
| D | ARG102 |
| D | THR185 |
| D | PHE204 |
| D | ASP211 |
| D | HIS232 |
| D | ALA233 |
| D | ARG280 |
| D | ARG308 |
| D | FAD401 |
| D | HOH520 |
| D | HOH616 |
| D | HOH642 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue FMT D 403 |
| Chain | Residue |
| D | SER37 |
| D | GLY38 |
| D | SER110 |
| D | THR113 |
| D | ARG114 |
| D | HOH573 |
| D | HOH604 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26016690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26016690","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
