3H3F
Rabbit muscle L-lactate dehydrogenase in complex with NADH and oxamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006089 | biological_process | lactate metabolic process |
| E | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006089 | biological_process | lactate metabolic process |
| F | 0006090 | biological_process | pyruvate metabolic 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006089 | biological_process | lactate metabolic process |
| G | 0006090 | biological_process | pyruvate metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0019752 | biological_process | carboxylic acid metabolic process |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006089 | biological_process | lactate metabolic process |
| H | 0006090 | biological_process | pyruvate metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAI A 332 |
| Chain | Residue |
| A | GLY28 |
| A | ILE115 |
| A | VAL135 |
| A | SER136 |
| A | ASN137 |
| A | HIS192 |
| A | ILE251 |
| A | OXM333 |
| A | HOH335 |
| A | HOH359 |
| A | HOH1075 |
| A | ALA29 |
| A | HOH1095 |
| A | HOH1117 |
| E | GLY102 |
| A | VAL30 |
| A | ASP51 |
| A | VAL52 |
| A | MET53 |
| A | THR94 |
| A | ALA95 |
| A | GLY96 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXM A 333 |
| Chain | Residue |
| A | ASN137 |
| A | ARG168 |
| A | HIS192 |
| A | ALA237 |
| A | THR247 |
| A | NAI332 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 334 |
| Chain | Residue |
| A | ASP42 |
| A | PHE70 |
| A | ARG72 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAI B 332 |
| Chain | Residue |
| B | GLY28 |
| B | ALA29 |
| B | VAL30 |
| B | ASP51 |
| B | VAL52 |
| B | MET53 |
| B | LYS56 |
| B | THR94 |
| B | ALA95 |
| B | GLY96 |
| B | ALA97 |
| B | ARG98 |
| B | VAL135 |
| B | ASN137 |
| B | LEU164 |
| B | HIS192 |
| B | THR247 |
| B | ILE251 |
| B | OXM333 |
| B | HOH336 |
| B | HOH339 |
| B | HOH344 |
| B | HOH347 |
| B | HOH364 |
| B | HOH365 |
| B | HOH422 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM B 333 |
| Chain | Residue |
| B | GLN99 |
| B | ARG105 |
| B | ASN137 |
| B | ARG168 |
| B | HIS192 |
| B | ALA237 |
| B | THR247 |
| B | NAI332 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 334 |
| Chain | Residue |
| B | LYS304 |
| B | VAL305 |
| B | HOH392 |
| B | HOH394 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAI C 332 |
| Chain | Residue |
| C | GLY28 |
| C | ALA29 |
| C | VAL30 |
| C | ASP51 |
| C | VAL52 |
| C | MET53 |
| C | LYS56 |
| C | THR94 |
| C | ALA95 |
| C | GLY96 |
| C | ALA97 |
| C | ARG98 |
| C | ILE119 |
| C | VAL135 |
| C | ASN137 |
| C | SER160 |
| C | HIS192 |
| C | THR247 |
| C | ILE251 |
| C | OXM333 |
| C | HOH351 |
| C | HOH352 |
| C | HOH366 |
| C | HOH368 |
| C | HOH555 |
| C | HOH729 |
| C | HOH730 |
| C | HOH776 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM C 333 |
| Chain | Residue |
| C | ASN137 |
| C | ARG168 |
| C | HIS192 |
| C | ALA237 |
| C | THR247 |
| C | NAI332 |
| C | GLN99 |
| C | ARG105 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 334 |
| Chain | Residue |
| C | ASN87 |
| C | SER88 |
| C | SER127 |
| C | PRO128 |
| C | HIS129 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT C 335 |
| Chain | Residue |
| C | LEU243 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAI D 332 |
| Chain | Residue |
| D | GLY26 |
| D | GLY28 |
| D | ALA29 |
| D | VAL30 |
| D | ASP51 |
| D | VAL52 |
| D | MET53 |
| D | TYR82 |
| D | THR94 |
| D | ALA95 |
| D | PHE118 |
| D | ILE119 |
| D | VAL135 |
| D | SER136 |
| D | ASN137 |
| D | VAL139 |
| D | SER160 |
| D | HOH567 |
| D | HOH645 |
| D | HOH731 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OXM D 333 |
| Chain | Residue |
| D | ASN137 |
| D | ARG168 |
| D | HIS192 |
| D | ALA237 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT D 334 |
| Chain | Residue |
| D | LYS316 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT D 335 |
| Chain | Residue |
| D | GLY281 |
| D | GLU312 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT D 336 |
| Chain | Residue |
| D | LYS316 |
| D | ACT337 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 337 |
| Chain | Residue |
| D | SER309 |
| D | GLU312 |
| D | ALA313 |
| D | ACT336 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 338 |
| Chain | Residue |
| D | MET40 |
| D | ASP42 |
| D | PHE70 |
| site_id | BC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAI E 332 |
| Chain | Residue |
| E | GLY28 |
| E | ALA29 |
| E | VAL30 |
| E | ASP51 |
| E | VAL52 |
| E | MET53 |
| E | THR94 |
| E | ALA95 |
| E | GLY96 |
| E | ILE115 |
| E | VAL135 |
| E | ASN137 |
| E | HIS192 |
| E | THR247 |
| E | ILE251 |
| E | OXM333 |
| E | HOH433 |
| E | HOH568 |
| E | HOH1054 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OXM E 333 |
| Chain | Residue |
| E | ASN137 |
| E | LEU164 |
| E | ARG168 |
| E | HIS192 |
| E | ALA237 |
| E | THR247 |
| E | NAI332 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT E 334 |
| Chain | Residue |
| E | LEU182 |
| E | HIS185 |
| E | HOH357 |
| E | HOH532 |
| G | ARG170 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT E 335 |
| Chain | Residue |
| E | ASP42 |
| E | PHE70 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT E 336 |
| Chain | Residue |
| E | ARG267 |
| E | HOH884 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT E 337 |
| Chain | Residue |
| E | LYS242 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT E 338 |
| Chain | Residue |
| E | ASP42 |
| H | ASP42 |
| H | ACT337 |
| site_id | CC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAI F 332 |
| Chain | Residue |
| B | ASN107 |
| F | GLY28 |
| F | ALA29 |
| F | VAL30 |
| F | ASP51 |
| F | VAL52 |
| F | MET53 |
| F | LYS56 |
| F | THR94 |
| F | ALA95 |
| F | GLY96 |
| F | ALA97 |
| F | ARG98 |
| F | VAL135 |
| F | ASN137 |
| F | SER160 |
| F | HIS192 |
| F | THR247 |
| F | ILE251 |
| F | OXM333 |
| F | HOH341 |
| F | HOH343 |
| F | HOH351 |
| F | HOH352 |
| F | HOH353 |
| F | HOH390 |
| F | HOH395 |
| F | HOH447 |
| F | HOH1065 |
| site_id | CC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM F 333 |
| Chain | Residue |
| F | GLN99 |
| F | ARG105 |
| F | ASN137 |
| F | ARG168 |
| F | HIS192 |
| F | ALA237 |
| F | THR247 |
| F | NAI332 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT F 334 |
| Chain | Residue |
| F | MET40 |
| F | PHE70 |
| F | ARG72 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT F 335 |
| Chain | Residue |
| F | HIS16 |
| F | HOH1191 |
| site_id | DC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAI G 332 |
| Chain | Residue |
| G | GLY28 |
| G | ALA29 |
| G | VAL30 |
| G | ASP51 |
| G | MET53 |
| G | LYS56 |
| G | THR94 |
| G | ALA95 |
| G | GLY96 |
| G | ALA97 |
| G | ARG98 |
| G | ILE119 |
| G | VAL135 |
| G | SER136 |
| G | ASN137 |
| G | SER160 |
| G | HIS192 |
| G | THR247 |
| G | ILE251 |
| G | OXM333 |
| G | HOH347 |
| G | HOH350 |
| G | HOH354 |
| G | HOH367 |
| G | HOH369 |
| G | HOH378 |
| G | HOH717 |
| site_id | DC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM G 333 |
| Chain | Residue |
| G | GLN99 |
| G | ARG105 |
| G | ASN137 |
| G | ARG168 |
| G | HIS192 |
| G | ALA237 |
| G | THR247 |
| G | NAI332 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT G 334 |
| Chain | Residue |
| G | ASP42 |
| G | PHE70 |
| G | LEU71 |
| G | ARG72 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT G 335 |
| Chain | Residue |
| G | LEU213 |
| G | HIS214 |
| G | PRO215 |
| G | LYS223 |
| H | GLN6 |
| site_id | DC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT G 336 |
| Chain | Residue |
| G | LEU329 |
| G | GLN330 |
| G | PHE331 |
| site_id | DC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI H 332 |
| Chain | Residue |
| D | GLN330 |
| H | GLY28 |
| H | ALA29 |
| H | VAL30 |
| H | ASP51 |
| H | VAL52 |
| H | MET53 |
| H | THR94 |
| H | ALA95 |
| H | GLY96 |
| H | ARG98 |
| H | ILE115 |
| H | VAL135 |
| H | ASN137 |
| H | HIS192 |
| H | THR247 |
| H | OXM333 |
| H | HOH341 |
| H | HOH344 |
| H | HOH369 |
| H | HOH372 |
| H | HOH572 |
| H | HOH849 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXM H 333 |
| Chain | Residue |
| H | ASN137 |
| H | ARG168 |
| H | HIS192 |
| H | ALA237 |
| H | THR247 |
| H | NAI332 |
| site_id | DC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT H 334 |
| Chain | Residue |
| H | VAL305 |
| H | HOH853 |
| site_id | EC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT H 335 |
| Chain | Residue |
| H | MET40 |
| H | ASP42 |
| site_id | EC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT H 336 |
| Chain | Residue |
| H | LYS4 |
| site_id | EC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT H 337 |
| Chain | Residue |
| E | ACT338 |
| H | LYS41 |
| H | GLU260 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
| Chain | Residue | Details |
| A | LEU189-SER195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19715328 |
| Chain | Residue | Details |
| A | HIS192 | |
| B | HIS192 | |
| C | HIS192 | |
| D | HIS192 | |
| E | HIS192 | |
| F | HIS192 | |
| G | HIS192 | |
| H | HIS192 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY28 | |
| B | ASN137 | |
| B | ARG168 | |
| B | THR247 | |
| C | GLY28 | |
| C | ARG98 | |
| C | ARG105 | |
| C | ASN137 | |
| C | ARG168 | |
| C | THR247 | |
| D | GLY28 | |
| A | ARG98 | |
| D | ARG98 | |
| D | ARG105 | |
| D | ASN137 | |
| D | ARG168 | |
| D | THR247 | |
| E | GLY28 | |
| E | ARG98 | |
| E | ARG105 | |
| E | ASN137 | |
| E | ARG168 | |
| A | ARG105 | |
| E | THR247 | |
| F | GLY28 | |
| F | ARG98 | |
| F | ARG105 | |
| F | ASN137 | |
| F | ARG168 | |
| F | THR247 | |
| G | GLY28 | |
| G | ARG98 | |
| G | ARG105 | |
| A | ASN137 | |
| G | ASN137 | |
| G | ARG168 | |
| G | THR247 | |
| H | GLY28 | |
| H | ARG98 | |
| H | ARG105 | |
| H | ASN137 | |
| H | ARG168 | |
| H | THR247 | |
| A | ARG168 | |
| A | THR247 | |
| B | GLY28 | |
| B | ARG98 | |
| B | ARG105 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P00338 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 | |
| C | ALA1 | |
| D | ALA1 | |
| E | ALA1 | |
| F | ALA1 | |
| G | ALA1 | |
| H | ALA1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 |
| Chain | Residue | Details |
| A | LYS4 | |
| D | LYS4 | |
| D | LYS117 | |
| D | LYS317 | |
| E | LYS4 | |
| E | LYS117 | |
| E | LYS317 | |
| F | LYS4 | |
| F | LYS117 | |
| F | LYS317 | |
| G | LYS4 | |
| A | LYS117 | |
| G | LYS117 | |
| G | LYS317 | |
| H | LYS4 | |
| H | LYS117 | |
| H | LYS317 | |
| A | LYS317 | |
| B | LYS4 | |
| B | LYS117 | |
| B | LYS317 | |
| C | LYS4 | |
| C | LYS117 | |
| C | LYS317 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00338 |
| Chain | Residue | Details |
| A | LYS13 | |
| D | LYS13 | |
| D | LYS80 | |
| D | LYS125 | |
| E | LYS13 | |
| E | LYS80 | |
| E | LYS125 | |
| F | LYS13 | |
| F | LYS80 | |
| F | LYS125 | |
| G | LYS13 | |
| A | LYS80 | |
| G | LYS80 | |
| G | LYS125 | |
| H | LYS13 | |
| H | LYS80 | |
| H | LYS125 | |
| A | LYS125 | |
| B | LYS13 | |
| B | LYS80 | |
| B | LYS125 | |
| C | LYS13 | |
| C | LYS80 | |
| C | LYS125 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 |
| Chain | Residue | Details |
| A | LYS56 | |
| B | LYS56 | |
| C | LYS56 | |
| D | LYS56 | |
| E | LYS56 | |
| F | LYS56 | |
| G | LYS56 | |
| H | LYS56 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151 |
| Chain | Residue | Details |
| A | LYS223 | |
| D | LYS223 | |
| D | LYS231 | |
| D | LYS242 | |
| E | LYS223 | |
| E | LYS231 | |
| E | LYS242 | |
| F | LYS223 | |
| F | LYS231 | |
| F | LYS242 | |
| G | LYS223 | |
| A | LYS231 | |
| G | LYS231 | |
| G | LYS242 | |
| H | LYS223 | |
| H | LYS231 | |
| H | LYS242 | |
| A | LYS242 | |
| B | LYS223 | |
| B | LYS231 | |
| B | LYS242 | |
| C | LYS223 | |
| C | LYS231 | |
| C | LYS242 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151 |
| Chain | Residue | Details |
| A | TYR238 | |
| B | TYR238 | |
| C | TYR238 | |
| D | TYR238 | |
| E | TYR238 | |
| F | TYR238 | |
| G | TYR238 | |
| H | TYR238 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642 |
| Chain | Residue | Details |
| A | THR308 | |
| E | THR321 | |
| F | THR308 | |
| F | THR321 | |
| G | THR308 | |
| G | THR321 | |
| H | THR308 | |
| H | THR321 | |
| A | THR321 | |
| B | THR308 | |
| B | THR321 | |
| C | THR308 | |
| C | THR321 | |
| D | THR308 | |
| D | THR321 | |
| E | THR308 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00338 |
| Chain | Residue | Details |
| A | SER309 | |
| B | SER309 | |
| C | SER309 | |
| D | SER309 | |
| E | SER309 | |
| F | SER309 | |
| G | SER309 | |
| H | SER309 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 16 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P00338 |
| Chain | Residue | Details |
| A | LYS56 | |
| F | LYS56 | |
| G | LYS56 | |
| H | LYS56 | |
| B | LYS56 | |
| C | LYS56 | |
| D | LYS56 | |
| E | LYS56 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS192 | |
| A | ASP165 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS192 | |
| B | ASP165 | |
| B | ARG168 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS192 | |
| C | ASP165 | |
| C | ARG168 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS192 | |
| D | ASP165 | |
| D | ARG168 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | HIS192 | |
| E | ASP165 | |
| E | ARG168 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | HIS192 | |
| F | ASP165 | |
| F | ARG168 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | HIS192 | |
| G | ASP165 | |
| G | ARG168 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | HIS192 | |
| H | ASP165 | |
| H | ARG168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS192 | |
| B | ASP165 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS192 | |
| C | ASP165 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS192 | |
| D | ASP165 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | HIS192 | |
| E | ASP165 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | HIS192 | |
| F | ASP165 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | HIS192 | |
| G | ASP165 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | HIS192 | |
| H | ASP165 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS192 | |
| A | ASP165 | |
| A | ARG168 |
