1Z7E
Crystal structure of full length ArnA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009245 | biological_process | lipid A 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 | 0016740 | molecular_function | transferase activity |
| A | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046493 | biological_process | lipid A metabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| A | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| A | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009245 | biological_process | lipid A 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 | 0016740 | molecular_function | transferase activity |
| B | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046493 | biological_process | lipid A metabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| B | 0070403 | molecular_function | NAD+ binding |
| B | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| B | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| B | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0009245 | biological_process | lipid A biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046493 | biological_process | lipid A metabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| C | 0070403 | molecular_function | NAD+ binding |
| C | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| C | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| C | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0009245 | biological_process | lipid A biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046493 | biological_process | lipid A metabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| D | 0070403 | molecular_function | NAD+ binding |
| D | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| D | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| D | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| E | 0009245 | biological_process | lipid A biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| E | 0016831 | molecular_function | carboxy-lyase activity |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046493 | biological_process | lipid A metabolic process |
| E | 0046677 | biological_process | response to antibiotic |
| E | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| E | 0070403 | molecular_function | NAD+ binding |
| E | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| E | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| E | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| F | 0009245 | biological_process | lipid A biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| F | 0016831 | molecular_function | carboxy-lyase activity |
| F | 0032991 | cellular_component | protein-containing complex |
| F | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046493 | biological_process | lipid A metabolic process |
| F | 0046677 | biological_process | response to antibiotic |
| F | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| F | 0070403 | molecular_function | NAD+ binding |
| F | 0099618 | molecular_function | UDP-glucuronic acid dehydrogenase activity |
| F | 0099619 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity |
| F | 2001315 | biological_process | UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP A 1001 |
| Chain | Residue |
| A | ASN324 |
| A | LEU389 |
| A | VAL390 |
| A | ALA393 |
| A | ARG510 |
| A | GLY325 |
| A | PHE326 |
| A | ILE327 |
| A | ASP347 |
| A | ILE348 |
| A | GLY367 |
| A | ASP368 |
| A | ILE369 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP B 1002 |
| Chain | Residue |
| B | ASN324 |
| B | GLY325 |
| B | PHE326 |
| B | ILE327 |
| B | ASP347 |
| B | ILE348 |
| B | GLY367 |
| B | ASP368 |
| B | ILE369 |
| B | LEU389 |
| B | VAL390 |
| B | ALA393 |
| B | ARG510 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ATP C 1003 |
| Chain | Residue |
| C | GLY322 |
| C | GLY325 |
| C | PHE326 |
| C | ILE327 |
| C | ASP347 |
| C | ILE348 |
| C | GLY367 |
| C | ASP368 |
| C | ILE369 |
| C | LEU389 |
| C | VAL390 |
| C | ARG510 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP D 1004 |
| Chain | Residue |
| D | GLY325 |
| D | PHE326 |
| D | ILE327 |
| D | ASP347 |
| D | ILE348 |
| D | GLY367 |
| D | ASP368 |
| D | ILE369 |
| D | LEU389 |
| D | VAL390 |
| D | ARG510 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP E 1005 |
| Chain | Residue |
| E | GLY325 |
| E | PHE326 |
| E | ILE327 |
| E | ASP347 |
| E | ILE348 |
| E | GLY367 |
| E | ASP368 |
| E | ILE369 |
| E | LEU389 |
| E | VAL390 |
| E | ARG510 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP F 1006 |
| Chain | Residue |
| F | ASN324 |
| F | GLY325 |
| F | PHE326 |
| F | ILE327 |
| F | ASP347 |
| F | ILE348 |
| F | GLY367 |
| F | ASP368 |
| F | ILE369 |
| F | LEU389 |
| F | VAL390 |
| F | ALA393 |
| F | ARG510 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA A 1101 |
| Chain | Residue |
| A | ALA393 |
| A | PRO395 |
| A | TYR398 |
| A | THR432 |
| A | SER433 |
| A | GLU434 |
| A | ARG460 |
| A | TYR463 |
| A | PRO490 |
| A | PHE491 |
| A | ASN492 |
| A | ARG510 |
| A | ALA511 |
| A | GLN514 |
| A | LYS526 |
| A | LEU527 |
| A | ILE528 |
| A | GLN533 |
| A | ARG535 |
| A | ILE574 |
| A | TYR609 |
| A | TYR613 |
| A | ASP615 |
| A | ARG619 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA B 1102 |
| Chain | Residue |
| B | TYR398 |
| B | THR432 |
| B | SER433 |
| B | GLU434 |
| B | ARG460 |
| B | TYR463 |
| B | PRO490 |
| B | PHE491 |
| B | ASN492 |
| B | ARG510 |
| B | ALA511 |
| B | GLN514 |
| B | LYS526 |
| B | LEU527 |
| B | ILE528 |
| B | GLN533 |
| B | ARG535 |
| B | ILE574 |
| B | TYR609 |
| B | TYR613 |
| B | ASP615 |
| B | ARG619 |
| B | ALA393 |
| B | PRO395 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA C 1103 |
| Chain | Residue |
| C | ALA393 |
| C | PRO395 |
| C | TYR398 |
| C | THR432 |
| C | SER433 |
| C | GLU434 |
| C | ARG460 |
| C | TYR463 |
| C | PRO490 |
| C | PHE491 |
| C | ASN492 |
| C | ARG510 |
| C | ALA511 |
| C | GLN514 |
| C | LYS526 |
| C | LEU527 |
| C | ILE528 |
| C | GLN533 |
| C | ARG535 |
| C | ILE574 |
| C | TYR609 |
| C | TYR613 |
| C | ASP615 |
| C | ARG619 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA D 1104 |
| Chain | Residue |
| D | ALA393 |
| D | PRO395 |
| D | TYR398 |
| D | THR432 |
| D | SER433 |
| D | GLU434 |
| D | ARG460 |
| D | TYR463 |
| D | PRO490 |
| D | PHE491 |
| D | ASN492 |
| D | ARG510 |
| D | ALA511 |
| D | GLN514 |
| D | LYS526 |
| D | LEU527 |
| D | ILE528 |
| D | GLN533 |
| D | ARG535 |
| D | ILE574 |
| D | TYR609 |
| D | TYR613 |
| D | ASP615 |
| D | ARG619 |
| site_id | BC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA E 1105 |
| Chain | Residue |
| E | ALA393 |
| E | PRO395 |
| E | TYR398 |
| E | THR432 |
| E | SER433 |
| E | GLU434 |
| E | ARG460 |
| E | TYR463 |
| E | PRO490 |
| E | PHE491 |
| E | ASN492 |
| E | ARG510 |
| E | ALA511 |
| E | GLN514 |
| E | LYS526 |
| E | LEU527 |
| E | ILE528 |
| E | GLN533 |
| E | ARG535 |
| E | ILE574 |
| E | TYR609 |
| E | TYR613 |
| E | ASP615 |
| E | ARG619 |
| site_id | BC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UGA F 1106 |
| Chain | Residue |
| F | ALA393 |
| F | PRO395 |
| F | TYR398 |
| F | THR432 |
| F | SER433 |
| F | GLU434 |
| F | ARG460 |
| F | TYR463 |
| F | PRO490 |
| F | PHE491 |
| F | ASN492 |
| F | ARG510 |
| F | ALA511 |
| F | GLN514 |
| F | LYS526 |
| F | LEU527 |
| F | ILE528 |
| F | GLN533 |
| F | ARG535 |
| F | ILE574 |
| F | TYR609 |
| F | TYR613 |
| F | ASP615 |
| F | ARG619 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor; for formyltransferase activity |
| Chain | Residue | Details |
| A | HIS104 | |
| B | HIS104 | |
| C | HIS104 | |
| D | HIS104 | |
| E | HIS104 | |
| F | HIS104 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor; for decarboxylase activity |
| Chain | Residue | Details |
| A | GLU434 | |
| B | GLU434 | |
| C | GLU434 | |
| D | GLU434 | |
| E | GLU434 | |
| F | GLU434 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor; for decarboxylase activity |
| Chain | Residue | Details |
| A | ARG619 | |
| B | ARG619 | |
| C | ARG619 | |
| D | ARG619 | |
| E | ARG619 | |
| F | ARG619 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 72 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS86 | |
| A | ASN492 | |
| A | LYS526 | |
| A | TYR613 | |
| B | HIS86 | |
| B | ARG114 | |
| B | VAL136 | |
| B | ASP347 | |
| B | ASP368 | |
| B | ALA393 | |
| B | TYR398 | |
| A | ARG114 | |
| B | THR432 | |
| B | ARG460 | |
| B | ASN492 | |
| B | LYS526 | |
| B | TYR613 | |
| C | HIS86 | |
| C | ARG114 | |
| C | VAL136 | |
| C | ASP347 | |
| C | ASP368 | |
| A | VAL136 | |
| C | ALA393 | |
| C | TYR398 | |
| C | THR432 | |
| C | ARG460 | |
| C | ASN492 | |
| C | LYS526 | |
| C | TYR613 | |
| D | HIS86 | |
| D | ARG114 | |
| D | VAL136 | |
| A | ASP347 | |
| D | ASP347 | |
| D | ASP368 | |
| D | ALA393 | |
| D | TYR398 | |
| D | THR432 | |
| D | ARG460 | |
| D | ASN492 | |
| D | LYS526 | |
| D | TYR613 | |
| E | HIS86 | |
| A | ASP368 | |
| E | ARG114 | |
| E | VAL136 | |
| E | ASP347 | |
| E | ASP368 | |
| E | ALA393 | |
| E | TYR398 | |
| E | THR432 | |
| E | ARG460 | |
| E | ASN492 | |
| E | LYS526 | |
| A | ALA393 | |
| E | TYR613 | |
| F | HIS86 | |
| F | ARG114 | |
| F | VAL136 | |
| F | ASP347 | |
| F | ASP368 | |
| F | ALA393 | |
| F | TYR398 | |
| F | THR432 | |
| F | ARG460 | |
| A | TYR398 | |
| F | ASN492 | |
| F | LYS526 | |
| F | TYR613 | |
| A | THR432 | |
| A | ARG460 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ASN102 | |
| B | ASN102 | |
| C | ASN102 | |
| D | ASN102 | |
| E | ASN102 | |
| F | ASN102 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | SITE: Raises pKa of active site His |
| Chain | Residue | Details |
| A | ASP140 | |
| B | ASP140 | |
| C | ASP140 | |
| D | ASP140 | |
| E | ASP140 | |
| F | ASP140 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASN102 | |
| A | HIS104 | |
| A | THR131 | |
| A | ASP140 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASN102 | |
| D | HIS104 | |
| D | ASP140 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| E | ASN102 | |
| E | HIS104 | |
| E | ASP140 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| F | ASN102 | |
| F | HIS104 | |
| F | ASP140 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | TYR463 | |
| A | LYS467 | |
| A | THR432 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | TYR463 | |
| B | LYS467 | |
| B | THR432 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | TYR463 | |
| C | LYS467 | |
| C | THR432 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | TYR463 | |
| D | LYS467 | |
| D | THR432 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| E | TYR463 | |
| E | LYS467 | |
| E | THR432 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| F | TYR463 | |
| F | LYS467 | |
| F | THR432 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | HIS104 | |
| A | ASP140 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASN102 | |
| B | HIS104 | |
| B | THR131 | |
| B | ASP140 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | HIS104 | |
| B | ASP140 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | HIS104 | |
| C | ASP140 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | HIS104 | |
| D | ASP140 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| E | HIS104 | |
| E | ASP140 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| F | HIS104 | |
| F | ASP140 |
| site_id | CSA25 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | TYR463 | |
| A | THR432 | |
| A | LYS467 | |
| A | GLU434 |
| site_id | CSA26 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | TYR463 | |
| B | THR432 | |
| B | LYS467 | |
| B | GLU434 |
| site_id | CSA27 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | TYR463 | |
| C | THR432 | |
| C | LYS467 | |
| C | GLU434 |
| site_id | CSA28 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | TYR463 | |
| D | THR432 | |
| D | LYS467 | |
| D | GLU434 |
| site_id | CSA29 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| E | TYR463 | |
| E | THR432 | |
| E | LYS467 | |
| E | GLU434 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASN102 | |
| C | HIS104 | |
| C | THR131 | |
| C | ASP140 |
| site_id | CSA30 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| F | TYR463 | |
| F | THR432 | |
| F | LYS467 | |
| F | GLU434 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASN102 | |
| D | HIS104 | |
| D | THR131 | |
| D | ASP140 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| E | ASN102 | |
| E | HIS104 | |
| E | THR131 | |
| E | ASP140 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| F | ASN102 | |
| F | HIS104 | |
| F | THR131 | |
| F | ASP140 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASN102 | |
| A | HIS104 | |
| A | ASP140 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASN102 | |
| B | HIS104 | |
| B | ASP140 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASN102 | |
| C | HIS104 | |
| C | ASP140 |
