4KTT
Structural insights of MAT enzymes: MATa2b complexed with SAM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048269 | cellular_component | methionine adenosyltransferase complex |
| A | 0051291 | biological_process | protein heterooligomerization |
| A | 0061431 | biological_process | cellular response to methionine |
| A | 1904263 | biological_process | positive regulation of TORC1 signaling |
| A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048269 | cellular_component | methionine adenosyltransferase complex |
| B | 0051291 | biological_process | protein heterooligomerization |
| B | 0061431 | biological_process | cellular response to methionine |
| B | 1904263 | biological_process | positive regulation of TORC1 signaling |
| B | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0036094 | molecular_function | small molecule binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048269 | cellular_component | methionine adenosyltransferase complex |
| C | 0051291 | biological_process | protein heterooligomerization |
| C | 0061431 | biological_process | cellular response to methionine |
| C | 1904263 | biological_process | positive regulation of TORC1 signaling |
| C | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0034214 | biological_process | protein hexamerization |
| D | 0036094 | molecular_function | small molecule binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048269 | cellular_component | methionine adenosyltransferase complex |
| D | 0051291 | biological_process | protein heterooligomerization |
| D | 0061431 | biological_process | cellular response to methionine |
| D | 1904263 | biological_process | positive regulation of TORC1 signaling |
| D | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005829 | cellular_component | cytosol |
| E | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| E | 0006730 | biological_process | one-carbon metabolic process |
| E | 0019899 | molecular_function | enzyme binding |
| E | 0048269 | cellular_component | methionine adenosyltransferase complex |
| E | 0048270 | molecular_function | methionine adenosyltransferase regulator activity |
| E | 0070062 | cellular_component | extracellular exosome |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005829 | cellular_component | cytosol |
| F | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| F | 0006730 | biological_process | one-carbon metabolic process |
| F | 0019899 | molecular_function | enzyme binding |
| F | 0048269 | cellular_component | methionine adenosyltransferase complex |
| F | 0048270 | molecular_function | methionine adenosyltransferase regulator activity |
| F | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | PHE333 |
| B | GLN190 |
| F | THR320 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| B | LEU346 |
| A | THR17 |
| A | HOH502 |
| A | HOH523 |
| B | SER331 |
| B | ILE332 |
| B | GLU342 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | ALA162 |
| A | ALA165 |
| A | ARG169 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | ARG168 |
| A | ARG177 |
| A | PRO178 |
| A | SER180 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAM A 405 |
| Chain | Residue |
| A | HIS29 |
| A | PRO30 |
| A | ASP179 |
| A | LYS181 |
| A | SER247 |
| A | ARG249 |
| A | PHE250 |
| A | ASP258 |
| B | ALA55 |
| B | GLU70 |
| B | GLN113 |
| B | ASP116 |
| B | ILE117 |
| B | GLY133 |
| B | ASP134 |
| B | LYS289 |
| B | HOH514 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 406 |
| Chain | Residue |
| A | HIS29 |
| A | ASP31 |
| A | ASP258 |
| A | ARG264 |
| B | LYS285 |
| B | ASP291 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 401 |
| Chain | Residue |
| B | ASP365 |
| B | LEU366 |
| B | LYS368 |
| B | ILE370 |
| B | TYR371 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| B | ALA162 |
| B | ARG169 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | GLY63 |
| B | PHE99 |
| B | ASP100 |
| B | THR103 |
| C | THR103 |
| C | CYS104 |
| C | HOH506 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 404 |
| Chain | Residue |
| B | ASP35 |
| B | ILE266 |
| B | ASP269 |
| B | ALA281 |
| B | PHE282 |
| B | SER283 |
| B | HOH512 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 405 |
| Chain | Residue |
| B | ASP78 |
| B | TYR79 |
| B | HOH516 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 406 |
| Chain | Residue |
| A | GLU57 |
| B | ASP31 |
| B | ALA259 |
| B | ARG264 |
| B | EDO407 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 407 |
| Chain | Residue |
| A | LYS285 |
| A | ASP291 |
| B | HIS29 |
| B | LYS265 |
| B | EDO406 |
| B | HOH519 |
| B | HOH520 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 408 |
| Chain | Residue |
| B | LEU137 |
| B | PHE139 |
| B | HIS277 |
| B | GLY278 |
| B | GLY280 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 409 |
| Chain | Residue |
| B | ARG192 |
| B | ARG312 |
| B | GLY336 |
| B | THR337 |
| F | TRP309 |
| F | PRO310 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 410 |
| Chain | Residue |
| B | ASP31 |
| B | ASP35 |
| B | LEU261 |
| B | THR262 |
| B | GLY263 |
| B | ARG264 |
| B | LYS265 |
| B | HOH512 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 401 |
| Chain | Residue |
| C | GLY278 |
| C | PHE139 |
| C | THR270 |
| C | TYR271 |
| C | ALA276 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| C | GLU27 |
| C | GLN36 |
| C | HIS89 |
| C | GLN372 |
| C | ARG373 |
| C | TYR377 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | PHE333 |
| C | HIS334 |
| C | TYR335 |
| E | THR320 |
| site_id | CC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAM C 404 |
| Chain | Residue |
| C | HIS29 |
| C | PRO30 |
| C | ASP179 |
| C | LYS181 |
| C | SER247 |
| C | ARG249 |
| C | PHE250 |
| C | GLY257 |
| C | ASP258 |
| C | PO4405 |
| D | ALA55 |
| D | GLU70 |
| D | GLN113 |
| D | ASP116 |
| D | ILE117 |
| D | GLY133 |
| D | ASP134 |
| D | LYS289 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 C 405 |
| Chain | Residue |
| C | HIS29 |
| C | ASP31 |
| C | LYS181 |
| C | ASP258 |
| C | LYS265 |
| C | SAM404 |
| D | ASP134 |
| D | ASP291 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 401 |
| Chain | Residue |
| D | SER95 |
| D | ILE252 |
| D | GLN256 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 402 |
| Chain | Residue |
| D | ASP144 |
| D | LYS307 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 403 |
| Chain | Residue |
| D | LYS340 |
| D | GLU344 |
| D | HOH524 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 404 |
| Chain | Residue |
| B | ASP78 |
| D | ILE71 |
| D | GLU111 |
| D | GLN112 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 405 |
| Chain | Residue |
| D | ARG192 |
| D | ARG312 |
| D | GLY336 |
| D | THR337 |
| E | TRP309 |
| site_id | CC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 406 |
| Chain | Residue |
| D | LEU46 |
| D | PRO50 |
| D | ASP51 |
| D | ALA52 |
| D | LYS53 |
| D | ASP286 |
| D | TYR287 |
| D | LEU366 |
| D | LYS367 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 407 |
| Chain | Residue |
| A | LYS61 |
| A | THR62 |
| B | GLU111 |
| D | GLN80 |
| D | ARG84 |
| D | CYS104 |
| D | ASN105 |
| D | VAL106 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 401 |
| Chain | Residue |
| E | PRO88 |
| E | ALA185 |
| E | ARG208 |
| E | LYS247 |
| E | ARG278 |
| E | HOH511 |
| site_id | DC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO E 402 |
| Chain | Residue |
| F | TRP205 |
| F | ILE268 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 403 |
| Chain | Residue |
| E | ASN242 |
| E | GLN283 |
| E | LEU284 |
| E | ARG297 |
| E | HOH502 |
| E | HOH504 |
| site_id | DC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO E 404 |
| Chain | Residue |
| E | ASN201 |
| E | MET202 |
| E | ASP203 |
| site_id | DC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO F 401 |
| Chain | Residue |
| F | HIS77 |
| F | HOH503 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2YDX |
| Chain | Residue | Details |
| E | ALA25 | |
| F | VAL59 | |
| F | HIS81 | |
| F | GLU85 | |
| F | LEU147 | |
| F | ILE173 | |
| E | GLY48 | |
| E | VAL59 | |
| E | HIS81 | |
| E | GLU85 | |
| E | LEU147 | |
| E | ILE173 | |
| F | ALA25 | |
| F | GLY48 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| E | ARG297 | |
| F | ARG297 | |
| C | ASP31 | |
| D | ASP31 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A817 |
| Chain | Residue | Details |
| A | GLU57 | |
| B | GLU57 | |
| C | GLU57 | |
| D | GLU57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
| Chain | Residue | Details |
| A | GLU70 | |
| B | GLU70 | |
| C | GLU70 | |
| D | GLU70 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:25075345 |
| Chain | Residue | Details |
| A | GLN113 | |
| B | GLN113 | |
| C | GLN113 | |
| D | GLN113 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I |
| Chain | Residue | Details |
| A | ASP179 | |
| B | ASP179 | |
| C | ASP179 | |
| D | ASP179 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I |
| Chain | Residue | Details |
| A | SER247 | |
| B | SER247 | |
| C | SER247 | |
| D | SER247 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1I |
| Chain | Residue | Details |
| A | ASP258 | |
| B | ASP258 | |
| C | ASP258 | |
| D | ASP258 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN |
| Chain | Residue | Details |
| A | ALA281 | |
| B | ALA281 | |
| C | ALA281 | |
| D | ALA281 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN |
| Chain | Residue | Details |
| A | LYS285 | |
| A | ASP291 | |
| B | LYS285 | |
| B | ASP291 | |
| C | LYS285 | |
| C | ASP291 | |
| D | LYS285 | |
| D | ASP291 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0A817 |
| Chain | Residue | Details |
| A | LYS289 | |
| B | LYS289 | |
| C | LYS289 | |
| D | LYS289 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS81 | |
| B | LYS81 | |
| C | LYS81 | |
| D | LYS81 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 | |
| C | SER114 | |
| D | SER114 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER384 | |
| B | SER384 | |
| C | SER384 | |
| D | SER384 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS228 | |
| D | LYS228 | |
| D | LYS234 | |
| A | LYS234 | |
| B | LYS228 | |
| B | LYS234 | |
| C | LYS228 | |
| C | LYS234 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 9 |
| Chain | Residue | Details |
| A | HIS29 | proton acceptor, proton donor |
| A | ARG264 | electrostatic stabiliser |
| A | LYS265 | electrostatic stabiliser |
| A | LYS285 | electrostatic stabiliser |
| A | LYS289 | electrostatic stabiliser |
| A | ASP291 | electrostatic stabiliser |
| A | ASP31 | electrostatic stabiliser, metal ligand |
| A | LYS32 | electrostatic stabiliser |
| A | GLU57 | metal ligand |
| A | GLU70 | electrostatic stabiliser, steric role |
| A | LYS181 | electrostatic stabiliser |
| A | PHE250 | steric role |
| A | ASP258 | electrostatic stabiliser, metal ligand, steric role |
| A | ALA259 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 14 |
| Details | M-CSA 9 |
| Chain | Residue | Details |
| B | HIS29 | proton acceptor, proton donor |
| B | ARG264 | electrostatic stabiliser |
| B | LYS265 | electrostatic stabiliser |
| B | LYS285 | electrostatic stabiliser |
| B | LYS289 | electrostatic stabiliser |
| B | ASP291 | electrostatic stabiliser |
| B | ASP31 | electrostatic stabiliser, metal ligand |
| B | LYS32 | electrostatic stabiliser |
| B | GLU57 | metal ligand |
| B | GLU70 | electrostatic stabiliser, steric role |
| B | LYS181 | electrostatic stabiliser |
| B | PHE250 | steric role |
| B | ASP258 | electrostatic stabiliser, metal ligand, steric role |
| B | ALA259 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 14 |
| Details | M-CSA 9 |
| Chain | Residue | Details |
| C | HIS29 | proton acceptor, proton donor |
| C | ARG264 | electrostatic stabiliser |
| C | LYS265 | electrostatic stabiliser |
| C | LYS285 | electrostatic stabiliser |
| C | LYS289 | electrostatic stabiliser |
| C | ASP291 | electrostatic stabiliser |
| C | ASP31 | electrostatic stabiliser, metal ligand |
| C | LYS32 | electrostatic stabiliser |
| C | GLU57 | metal ligand |
| C | GLU70 | electrostatic stabiliser, steric role |
| C | LYS181 | electrostatic stabiliser |
| C | PHE250 | steric role |
| C | ASP258 | electrostatic stabiliser, metal ligand, steric role |
| C | ALA259 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 14 |
| Details | M-CSA 9 |
| Chain | Residue | Details |
| D | HIS29 | proton acceptor, proton donor |
| D | ARG264 | electrostatic stabiliser |
| D | LYS265 | electrostatic stabiliser |
| D | LYS285 | electrostatic stabiliser |
| D | LYS289 | electrostatic stabiliser |
| D | ASP291 | electrostatic stabiliser |
| D | ASP31 | electrostatic stabiliser, metal ligand |
| D | LYS32 | electrostatic stabiliser |
| D | GLU57 | metal ligand |
| D | GLU70 | electrostatic stabiliser, steric role |
| D | LYS181 | electrostatic stabiliser |
| D | PHE250 | steric role |
| D | ASP258 | electrostatic stabiliser, metal ligand, steric role |
| D | ALA259 | metal ligand |
