4P69
Acek (D477A) ICDH complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0016791 | molecular_function | phosphatase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0016791 | molecular_function | phosphatase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006097 | biological_process | glyoxylate cycle |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006979 | biological_process | response to oxidative stress |
| 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 | 0022900 | biological_process | electron transport chain |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0097216 | molecular_function | guanosine tetraphosphate binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006097 | biological_process | glyoxylate cycle |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006979 | biological_process | response to oxidative stress |
| 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 | 0022900 | biological_process | electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
| D | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue AMP A 601 |
| Chain | Residue |
| A | SER101 |
| A | GLU376 |
| A | ASN104 |
| A | SER105 |
| A | HIS113 |
| A | LEU116 |
| A | LYS291 |
| A | LYS294 |
| A | THR295 |
| A | TYR298 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue ADP A 602 |
| Chain | Residue |
| A | PRO316 |
| A | GLY317 |
| A | ILE318 |
| A | GLY320 |
| A | VAL322 |
| A | MET323 |
| A | VAL325 |
| A | LYS336 |
| A | GLU416 |
| A | ARG417 |
| A | ARG418 |
| A | MET419 |
| A | LYS461 |
| A | ASN462 |
| A | TYR474 |
| A | ASP475 |
| A | ALA477 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | ILE318 |
| B | GLY320 |
| B | MET321 |
| B | VAL322 |
| B | MET323 |
| B | VAL325 |
| B | VAL334 |
| B | LYS336 |
| B | GLU416 |
| B | ARG417 |
| B | MET419 |
| B | ASP457 |
| B | LYS461 |
| B | ASN462 |
| B | ASP475 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue AMP B 602 |
| Chain | Residue |
| B | ASN104 |
| B | SER105 |
| B | HIS113 |
| B | LYS291 |
| B | LYS294 |
| B | THR295 |
| B | TYR298 |
| B | GLU376 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for Ligand GLU C 87 bound to SER C 3 |
| Chain | Residue |
| C | SER3 |
| C | VAL5 |
| C | TYR78 |
| C | PRO85 |
| C | ALA86 |
| C | THR88 |
| C | LEU89 |
| C | ASP90 |
| C | LEU91 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for Ligand GLU C 87 bound to SER C 3 |
| Chain | Residue |
| C | SER3 |
| C | VAL5 |
| C | TYR78 |
| C | PRO85 |
| C | ALA86 |
| C | THR88 |
| C | LEU89 |
| C | ASP90 |
| C | LEU91 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for Ligand THR C 271 bound to ASN C 268 |
| Chain | Residue |
| C | ASP221 |
| C | ASN268 |
| C | PRO269 |
| C | ASN270 |
| C | GLY272 |
| C | LYS273 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for Ligand ASP C 392 bound to ASN C 352 |
| Chain | Residue |
| C | ASN352 |
| C | THR390 |
| C | TYR391 |
| C | PHE393 |
| C | GLU394 |
| C | LEU396 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide TYR C 57 and ARG C 61 |
| Chain | Residue |
| C | GLU25 |
| C | VAL53 |
| C | GLU54 |
| C | LYS55 |
| C | ALA56 |
| C | LYS58 |
| C | GLY59 |
| C | GLU60 |
| C | LYS62 |
| C | TRP369 |
| C | ALA372 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD3 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD5 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD7 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD8 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide PHE C 178 and PHE D 178 |
| Chain | Residue |
| C | LYS174 |
| C | VAL175 |
| C | ILE176 |
| C | LYS177 |
| C | LEU179 |
| C | ARG180 |
| C | GLU182 |
| C | MET183 |
| D | LYS174 |
| D | VAL175 |
| D | ILE176 |
| D | LYS177 |
| D | LEU179 |
| D | ARG180 |
| D | GLU182 |
| D | MET183 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide ASP C 221 and LYS C 273 |
| Chain | Residue |
| C | ALA217 |
| C | ILE218 |
| C | ALA219 |
| C | ASN220 |
| C | ARG222 |
| C | ASN268 |
| C | THR271 |
| C | GLY272 |
| C | GLU274 |
| site_id | AE1 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide ASP C 221 and LYS C 273 |
| Chain | Residue |
| C | ALA217 |
| C | ILE218 |
| C | ALA219 |
| C | ASN220 |
| C | ARG222 |
| C | ASN268 |
| C | THR271 |
| C | GLY272 |
| C | GLU274 |
| site_id | AE2 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide GLU C 238 and MET C 302 |
| Chain | Residue |
| C | ASP158 |
| C | LYS199 |
| C | CYS201 |
| C | THR237 |
| C | GLY239 |
| C | ALA240 |
| C | PHE241 |
| C | LYS242 |
| C | CYS301 |
| C | ASN303 |
| C | LEU304 |
| C | ASN305 |
| C | GLY306 |
| site_id | AE3 |
| Number of Residues | 29 |
| Details | binding site for Di-peptide ASP C 283 and ASP D 307 |
| Chain | Residue |
| C | ARG153 |
| C | LYS230 |
| C | ILE281 |
| C | ALA282 |
| C | ALA284 |
| C | PHE285 |
| C | LEU286 |
| C | ASN303 |
| C | LEU304 |
| C | ASN305 |
| C | GLY306 |
| C | TYR308 |
| C | ILE309 |
| C | SER310 |
| C | ASP311 |
| D | ARG153 |
| D | ILE281 |
| D | ALA282 |
| D | ALA284 |
| D | PHE285 |
| D | LEU286 |
| D | ASN303 |
| D | LEU304 |
| D | ASN305 |
| D | GLY306 |
| D | TYR308 |
| D | ILE309 |
| D | SER310 |
| D | ASP311 |
| site_id | AE4 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide LYS D 13 and GLU D 94 |
| Chain | Residue |
| D | LYS12 |
| D | ILE14 |
| D | THR15 |
| D | ASP90 |
| D | LEU91 |
| D | ILE92 |
| D | ARG93 |
| D | TYR95 |
| D | ARG96 |
| site_id | AE5 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 57 and ARG D 61 |
| Chain | Residue |
| D | GLU25 |
| D | VAL53 |
| D | LYS55 |
| D | ALA56 |
| D | LYS58 |
| D | GLY59 |
| D | GLU60 |
| D | LYS62 |
| D | TRP369 |
| D | THR370 |
| D | GLU371 |
| D | ALA372 |
| site_id | AE6 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 78 and GLU D 87 |
| Chain | Residue |
| D | SER3 |
| D | LYS4 |
| D | SER74 |
| D | VAL77 |
| D | GLY79 |
| D | VAL82 |
| D | PRO85 |
| D | ALA86 |
| D | THR88 |
| D | LEU89 |
| D | ASP90 |
| D | LEU91 |
| site_id | AE7 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AE8 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AE9 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF1 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF2 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF3 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF4 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF5 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide TYR D 125 and ARG D 208 |
| Chain | Residue |
| D | ASP123 |
| D | LEU124 |
| D | ILE126 |
| D | GLU154 |
| D | ASN155 |
| D | GLU204 |
| D | GLY205 |
| D | THR206 |
| D | LYS207 |
| D | LEU209 |
| D | ILE328 |
| D | ASP330 |
| site_id | AF6 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide GLN D 287 and LEU D 291 |
| Chain | Residue |
| C | ASP311 |
| D | ALA284 |
| D | PHE285 |
| D | LEU286 |
| D | GLN288 |
| D | ILE289 |
| D | LEU290 |
| D | ARG292 |
| D | PRO293 |
| site_id | AF7 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide GLU D 361 and ARG D 365 |
| Chain | Residue |
| D | ASN220 |
| D | ILE357 |
| D | LEU358 |
| D | SER359 |
| D | ALA360 |
| D | MET362 |
| D | MET363 |
| D | LEU364 |
| D | HIS366 |
| D | MET367 |
| D | GLY368 |
| D | ASP374 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI |
| Chain | Residue | Details |
| C | ASN303-ILE322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR |
| Chain | Residue | Details |
| C | THR104 | |
| D | THR104 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| C | SER113 | |
| C | ASN115 | |
| C | ARG129 | |
| C | ARG153 | |
| D | SER113 | |
| D | ASN115 | |
| D | ARG129 | |
| D | ARG153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| C | ARG119 | |
| D | ARG119 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDC, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| C | ASP307 | |
| D | ASP307 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:1ISO, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| C | HIS339 | |
| D | HIS339 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| C | ASN352 | |
| C | TYR391 | |
| D | ASN352 | |
| D | TYR391 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| C | ARG395 | |
| D | ARG395 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 |
| Chain | Residue | Details |
| C | TYR160 | |
| C | LYS230 | |
| D | TYR160 | |
| D | LYS230 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| C | LYS100 | |
| C | LYS242 | |
| D | LYS100 | |
| D | LYS242 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144 |
| Chain | Residue | Details |
| C | SER113 | |
| D | SER113 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| C | LYS142 | |
| D | LYS142 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 7 |
| Chain | Residue | Details |
| C | TYR160 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | LYS230 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| C | ASP283 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ASP307 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 7 |
| Chain | Residue | Details |
| D | TYR160 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | LYS230 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| D | ASP283 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ASP307 | metal ligand |
