5TEQ
C20S C293G MUTANT N-TERMINAL HUMAN ATP CITRATE LYASE BOUND TO CITRATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue FLC A 901 |
| Chain | Residue |
| A | GLY309 |
| A | PO4902 |
| A | HOH1009 |
| A | SER343 |
| A | ALA345 |
| A | ASN346 |
| A | PHE347 |
| A | THR348 |
| A | ARG379 |
| A | VAL626 |
| A | GLY665 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 902 |
| Chain | Residue |
| A | GLY281 |
| A | GLY282 |
| A | GLY283 |
| A | SER308 |
| A | SER663 |
| A | GLY664 |
| A | GLY665 |
| A | HIS760 |
| A | FLC901 |
| A | HOH1159 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 903 |
| Chain | Residue |
| A | ASP257 |
| A | SER260 |
| A | ALA262 |
| A | HOH1216 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue FLC B 901 |
| Chain | Residue |
| B | GLY309 |
| B | SER343 |
| B | ALA345 |
| B | ASN346 |
| B | PHE347 |
| B | THR348 |
| B | ARG379 |
| B | VAL626 |
| B | GLY665 |
| B | PO4902 |
| B | HOH1030 |
| B | HOH1063 |
| B | HOH1086 |
| B | HOH1153 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PO4 B 902 |
| Chain | Residue |
| B | GLY281 |
| B | GLY282 |
| B | GLY283 |
| B | SER308 |
| B | SER663 |
| B | GLY664 |
| B | GLY665 |
| B | HIS760 |
| B | FLC901 |
| B | HOH1030 |
| B | HOH1076 |
| B | HOH1086 |
| B | HOH1116 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 903 |
| Chain | Residue |
| B | ASP257 |
| B | SER260 |
| B | ALA262 |
Functional Information from PROSITE/UniProt
| site_id | PS00399 |
| Number of Residues | 17 |
| Details | SUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GtcAtmfssevQFGHAG |
| Chain | Residue | Details |
| A | GLY746-GLY762 |
| site_id | PS01216 |
| Number of Residues | 30 |
| Details | SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGGMSnElnniisrttdGvyegVAIGGD |
| Chain | Residue | Details |
| A | SER661-ASP690 |
| site_id | PS01217 |
| Number of Residues | 25 |
| Details | SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GrIwtMvAGGGASvvysDtIgdl.GG |
| Chain | Residue | Details |
| A | GLY273-GLY297 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000305|PubMed:1371749 |
| Chain | Residue | Details |
| A | HIS760 | |
| B | HIS760 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22102020 |
| Chain | Residue | Details |
| A | LYS58 | |
| B | GLY67 | |
| B | PRO109 | |
| B | VAL111 | |
| B | GLU118 | |
| B | ASP216 | |
| A | ARG66 | |
| A | GLY67 | |
| A | PRO109 | |
| A | VAL111 | |
| A | GLU118 | |
| A | ASP216 | |
| B | LYS58 | |
| B | ARG66 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20558738, ECO:0000269|PubMed:22102020 |
| Chain | Residue | Details |
| A | ASP257 | |
| A | SER260 | |
| A | ALA262 | |
| B | ASP257 | |
| B | SER260 | |
| B | ALA262 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20558738 |
| Chain | Residue | Details |
| A | GLY309 | |
| B | ARG379 | |
| A | ASN346 | |
| A | THR348 | |
| A | TYR364 | |
| A | ARG379 | |
| B | GLY309 | |
| B | ASN346 | |
| B | THR348 | |
| B | TYR364 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU779 | |
| B | LEU779 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR131 | |
| B | TYR131 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q91V92 |
| Chain | Residue | Details |
| A | SER263 | |
| B | SER263 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P16638 |
| Chain | Residue | Details |
| A | THR447 | |
| B | THR447 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P16638 |
| Chain | Residue | Details |
| A | SER451 | |
| B | SER451 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 or BCKDK => ECO:0000269|PubMed:29779826, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER455 | |
| B | SER455 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER459 | |
| B | SER459 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER481 | |
| B | SER481 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:23932781 |
| Chain | Residue | Details |
| A | LYS540 | |
| B | LYS540 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:23932781, ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS546 | |
| A | LYS554 | |
| B | LYS546 | |
| B | LYS554 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | THR639 | |
| B | THR639 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER663 | |
| B | SER663 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | TYR682 | |
| B | TYR682 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27664236, ECO:0000305|PubMed:23932781 |
| Chain | Residue | Details |
| A | LYS540 | |
| A | LYS546 | |
| A | LYS554 | |
| B | LYS540 | |
| B | LYS546 | |
| B | LYS554 |
