2VIG
Crystal structure of human short-chain acyl CoA dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0046359 | biological_process | butyrate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0046359 | biological_process | butyrate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0046359 | biological_process | butyrate catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0046359 | biological_process | butyrate catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005759 | cellular_component | mitochondrial matrix |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0006631 | biological_process | fatty acid metabolic process |
| E | 0006635 | biological_process | fatty acid beta-oxidation |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| E | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| E | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| E | 0046359 | biological_process | butyrate catabolic process |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005759 | cellular_component | mitochondrial matrix |
| F | 0006629 | biological_process | lipid metabolic process |
| F | 0006631 | biological_process | fatty acid metabolic process |
| F | 0006635 | biological_process | fatty acid beta-oxidation |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| F | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| F | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| F | 0046359 | biological_process | butyrate catabolic process |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005739 | cellular_component | mitochondrion |
| G | 0005759 | cellular_component | mitochondrial matrix |
| G | 0006629 | biological_process | lipid metabolic process |
| G | 0006631 | biological_process | fatty acid metabolic process |
| G | 0006635 | biological_process | fatty acid beta-oxidation |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| G | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| G | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| G | 0046359 | biological_process | butyrate catabolic process |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005634 | cellular_component | nucleus |
| H | 0005739 | cellular_component | mitochondrion |
| H | 0005759 | cellular_component | mitochondrial matrix |
| H | 0006629 | biological_process | lipid metabolic process |
| H | 0006631 | biological_process | fatty acid metabolic process |
| H | 0006635 | biological_process | fatty acid beta-oxidation |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| H | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| H | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| H | 0046359 | biological_process | butyrate catabolic process |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | PHE152 |
| A | TYR391 |
| A | GLU392 |
| A | THR394 |
| A | GLU396 |
| A | LEU400 |
| A | HOH711 |
| A | HOH630 |
| A | HOH683 |
| A | HOH633 |
| A | HOH639 |
| A | LEU154 |
| A | HOH669 |
| B | ARG297 |
| B | PHE300 |
| B | LEU304 |
| B | LEU307 |
| B | GLN365 |
| B | ILE366 |
| B | GLY369 |
| B | HOH608 |
| C | GLN308 |
| A | SER155 |
| A | GLY160 |
| A | SER161 |
| A | TRP185 |
| A | THR187 |
| A | LYS230 |
| A | ILE387 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 600 |
| Chain | Residue |
| A | ARG297 |
| A | PHE300 |
| A | LEU304 |
| A | LEU307 |
| A | GLN365 |
| A | ILE366 |
| A | GLY369 |
| A | HOH603 |
| B | PHE152 |
| B | LEU154 |
| B | SER155 |
| B | GLY160 |
| B | SER161 |
| B | TRP185 |
| B | THR187 |
| B | LYS230 |
| B | ILE387 |
| B | ILE390 |
| B | TYR391 |
| B | GLU392 |
| B | THR394 |
| B | GLU396 |
| B | COS502 |
| B | HOH676 |
| B | HOH634 |
| B | HOH681 |
| B | HOH675 |
| B | HOH669 |
| D | GLN308 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE COS B 605 |
| Chain | Residue |
| A | PHE300 |
| B | GLY160 |
| B | SER161 |
| B | PHE261 |
| B | MET265 |
| B | GLN266 |
| B | LEU268 |
| B | ASP269 |
| B | ARG272 |
| B | ILE342 |
| B | GLU392 |
| B | GLY393 |
| B | ILE397 |
| B | FAD501 |
| B | HOH656 |
| B | HOH646 |
| B | HOH631 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD C 600 |
| Chain | Residue |
| D | PHE300 |
| D | LEU304 |
| D | LEU307 |
| D | GLN365 |
| D | ILE366 |
| D | GLY369 |
| D | HOH650 |
| A | GLN308 |
| C | PHE152 |
| C | LEU154 |
| C | SER155 |
| C | GLY160 |
| C | SER161 |
| C | TRP185 |
| C | THR187 |
| C | LYS230 |
| C | ILE387 |
| C | ILE390 |
| C | TYR391 |
| C | GLU392 |
| C | THR394 |
| C | GLU396 |
| C | LEU400 |
| C | COS502 |
| C | HOH653 |
| C | HOH649 |
| C | HOH625 |
| C | HOH633 |
| C | HOH651 |
| C | HOH671 |
| D | ARG297 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE COS C 605 |
| Chain | Residue |
| C | SER155 |
| C | GLY160 |
| C | SER161 |
| C | LEU268 |
| C | ARG272 |
| C | GLU392 |
| C | GLY393 |
| C | ILE397 |
| C | FAD501 |
| site_id | AC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD D 600 |
| Chain | Residue |
| B | GLN308 |
| C | ARG297 |
| C | PHE300 |
| C | LEU304 |
| C | LEU307 |
| C | VAL309 |
| C | GLN365 |
| C | ILE366 |
| C | GLY369 |
| C | HOH604 |
| D | PHE152 |
| D | LEU154 |
| D | SER155 |
| D | GLY160 |
| D | SER161 |
| D | TRP185 |
| D | ILE186 |
| D | THR187 |
| D | LYS230 |
| D | ILE387 |
| D | TYR391 |
| D | GLU392 |
| D | THR394 |
| D | GLU396 |
| D | LEU400 |
| D | COS502 |
| D | HOH652 |
| D | HOH645 |
| D | HOH671 |
| D | HOH657 |
| D | HOH619 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE COS D 605 |
| Chain | Residue |
| D | SER155 |
| D | GLY160 |
| D | SER161 |
| D | LEU268 |
| D | ARG272 |
| D | GLU392 |
| D | GLY393 |
| D | FAD501 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD E 600 |
| Chain | Residue |
| E | PHE152 |
| E | LEU154 |
| E | SER155 |
| E | GLY160 |
| E | SER161 |
| E | TRP185 |
| E | THR187 |
| E | LYS230 |
| E | ILE390 |
| E | TYR391 |
| E | GLU392 |
| E | THR394 |
| E | GLU396 |
| E | LEU400 |
| E | HOH685 |
| E | HOH688 |
| E | HOH616 |
| E | HOH646 |
| E | HOH707 |
| E | HOH655 |
| F | ARG297 |
| F | PHE300 |
| F | LEU304 |
| F | LEU307 |
| F | VAL309 |
| F | GLN365 |
| F | ILE366 |
| F | GLY369 |
| F | HOH604 |
| G | GLN308 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD F 600 |
| Chain | Residue |
| E | ARG297 |
| E | PHE300 |
| E | LEU304 |
| E | LEU307 |
| E | VAL309 |
| E | GLN365 |
| E | ILE366 |
| E | GLY369 |
| E | HOH613 |
| F | PHE152 |
| F | LEU154 |
| F | SER155 |
| F | GLY160 |
| F | SER161 |
| F | TRP185 |
| F | THR187 |
| F | LYS230 |
| F | TYR391 |
| F | GLU392 |
| F | THR394 |
| F | GLU396 |
| F | COS502 |
| F | HOH654 |
| F | HOH656 |
| F | HOH647 |
| F | HOH652 |
| F | HOH630 |
| H | GLN308 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE COS F 605 |
| Chain | Residue |
| F | SER155 |
| F | GLY160 |
| F | SER161 |
| F | LEU268 |
| F | ARG272 |
| F | GLU392 |
| F | GLY393 |
| F | FAD501 |
| F | HOH610 |
| site_id | BC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD G 600 |
| Chain | Residue |
| E | GLN308 |
| G | PHE152 |
| G | LEU154 |
| G | SER155 |
| G | GLY160 |
| G | SER161 |
| G | TRP185 |
| G | ILE186 |
| G | THR187 |
| G | LYS230 |
| G | ILE387 |
| G | ILE390 |
| G | TYR391 |
| G | GLU392 |
| G | THR394 |
| G | GLU396 |
| G | LEU400 |
| G | COS502 |
| G | HOH637 |
| G | HOH662 |
| G | HOH689 |
| G | HOH674 |
| G | HOH630 |
| H | ARG297 |
| H | PHE300 |
| H | LEU304 |
| H | LEU307 |
| H | GLN365 |
| H | ILE366 |
| H | GLY369 |
| H | HOH644 |
| site_id | BC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COS G 605 |
| Chain | Residue |
| G | GLY160 |
| G | SER161 |
| G | ALA163 |
| G | ASN207 |
| G | PHE261 |
| G | MET265 |
| G | GLN266 |
| G | LEU268 |
| G | ASP269 |
| G | ARG272 |
| G | ILE342 |
| G | GLU392 |
| G | GLY393 |
| G | VAL401 |
| G | FAD501 |
| G | HOH672 |
| G | HOH642 |
| G | HOH601 |
| G | HOH660 |
| H | PHE300 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD H 600 |
| Chain | Residue |
| F | GLN308 |
| G | ARG297 |
| G | PHE300 |
| G | LEU307 |
| G | GLN365 |
| G | ILE366 |
| G | GLY369 |
| G | HOH611 |
| H | PHE152 |
| H | LEU154 |
| H | SER155 |
| H | GLY160 |
| H | SER161 |
| H | TRP185 |
| H | ILE186 |
| H | THR187 |
| H | LYS230 |
| H | ILE387 |
| H | ILE390 |
| H | TYR391 |
| H | GLU392 |
| H | THR394 |
| H | GLU396 |
| H | LEU400 |
| H | HOH669 |
| H | HOH695 |
| H | HOH647 |
| H | HOH614 |
| H | HOH610 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO F1414 |
| Chain | Residue |
| F | GLN59 |
| F | PRO67 |
| F | GLN70 |
| F | HOH699 |
| F | HOH704 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D1414 |
| Chain | Residue |
| D | PRO67 |
| D | GLN70 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO E1414 |
| Chain | Residue |
| E | LEU65 |
| E | PRO67 |
| E | GLN70 |
| E | HOH680 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO H1414 |
| Chain | Residue |
| H | GLN59 |
| H | LEU65 |
| H | PRO67 |
| H | GLN70 |
| H | HOH635 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B1412 |
| Chain | Residue |
| B | GLN59 |
| B | PRO67 |
| B | GLN70 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D1415 |
| Chain | Residue |
| B | ARG330 |
| D | GLU322 |
| D | ARG325 |
| D | LEU326 |
| D | HOH702 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A1413 |
| Chain | Residue |
| A | GLU322 |
| A | ARG325 |
| A | LEU326 |
| C | ARG330 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E1415 |
| Chain | Residue |
| E | GLU322 |
| E | ARG325 |
| E | LEU326 |
| G | ARG330 |
| E | HOH633 |
| E | HOH700 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO H1415 |
| Chain | Residue |
| F | ARG330 |
| H | GLU322 |
| H | ARG325 |
| H | LEU326 |
| H | HOH700 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO E1416 |
| Chain | Residue |
| E | GLU156 |
| E | PRO157 |
| E | SER167 |
| E | GLY181 |
| E | THR182 |
| E | HOH706 |
| E | HOH689 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO F1415 |
| Chain | Residue |
| D | GLU134 |
| F | GLU134 |
| F | GLN135 |
| F | TRP139 |
| F | HOH702 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO F1416 |
| Chain | Residue |
| F | GLU156 |
| F | SER167 |
| F | THR168 |
| F | GLY181 |
| F | THR182 |
| F | HOH693 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P15651","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 112 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB14.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB14.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q07417","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 13 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q07417","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY271 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU392 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLU392 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLU392 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| E | GLU392 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| F | GLU392 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| G | GLU392 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| H | GLU392 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY271 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLY271 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLY271 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| E | GLY271 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| F | GLY271 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| G | GLY271 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| H | GLY271 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU392 |






