eF-site ID 4tnu-AB PDB Code 4tnu Chain A, B click to enlarge Title Human brain aspartoacylase mutant Y231C complex with intermediate analog (N-phosphonomethyl-L-aspartate) Classification HYDROLASE Compound Aspartoacylase Source Homo sapiens (Human) (ACY2_HUMAN) Sequence A:  HIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVK PFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYE VRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILE DSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRS IAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHF NEGKEFPPCAIEVYKIIEKVDCPRDENGEIAAIIHPNLQD QDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYY EKKEAFAKTTKLTLNAKSIRC B:  HIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVK PFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYE VRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILE DSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRS IAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHF NEGKEFPPCAIEVYKIIEKVDCPRDENGEIAAIIHPNLQD QDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYY EKKEAFAKTTKLTLNAKSIRC Description Functional site 1) chain A residue 21 type sequence H description binding site for residue ZN A 401 source : AC1 2) chain A residue 24 type sequence E description binding site for residue ZN A 401 source : AC1 3) chain A residue 116 type sequence H description binding site for residue ZN A 401 source : AC1 4) chain A residue 21 type sequence H description binding site for residue AS9 A 402 source : AC2 5) chain A residue 24 type sequence E description binding site for residue AS9 A 402 source : AC2 6) chain A residue 63 type sequence R description binding site for residue AS9 A 402 source : AC2 7) chain A residue 70 type sequence N description binding site for residue AS9 A 402 source : AC2 8) chain A residue 71 type sequence R description binding site for residue AS9 A 402 source : AC2 9) chain A residue 116 type sequence H description binding site for residue AS9 A 402 source : AC2 10) chain A residue 117 type sequence N description binding site for residue AS9 A 402 source : AC2 11) chain A residue 127 type sequence I description binding site for residue AS9 A 402 source : AC2 12) chain A residue 164 type sequence Y description binding site for residue AS9 A 402 source : AC2 13) chain A residue 168 type sequence R description binding site for residue AS9 A 402 source : AC2 14) chain A residue 178 type sequence E description binding site for residue AS9 A 402 source : AC2 15) chain A residue 285 type sequence E description binding site for residue AS9 A 402 source : AC2 16) chain A residue 288 type sequence Y description binding site for residue AS9 A 402 source : AC2 17) chain B residue 21 type sequence H description binding site for residue ZN B 401 source : AC3 18) chain B residue 24 type sequence E description binding site for residue ZN B 401 source : AC3 19) chain B residue 116 type sequence H description binding site for residue ZN B 401 source : AC3 20) chain B residue 21 type sequence H description binding site for residue AS9 B 402 source : AC4 21) chain B residue 24 type sequence E description binding site for residue AS9 B 402 source : AC4 22) chain B residue 63 type sequence R description binding site for residue AS9 B 402 source : AC4 23) chain B residue 70 type sequence N description binding site for residue AS9 B 402 source : AC4 24) chain B residue 71 type sequence R description binding site for residue AS9 B 402 source : AC4 25) chain B residue 116 type sequence H description binding site for residue AS9 B 402 source : AC4 26) chain B residue 117 type sequence N description binding site for residue AS9 B 402 source : AC4 27) chain B residue 164 type sequence Y description binding site for residue AS9 B 402 source : AC4 28) chain B residue 168 type sequence R description binding site for residue AS9 B 402 source : AC4 29) chain B residue 178 type sequence E description binding site for residue AS9 B 402 source : AC4 30) chain B residue 285 type sequence E description binding site for residue AS9 B 402 source : AC4 31) chain B residue 288 type sequence Y description binding site for residue AS9 B 402 source : AC4 32) chain A residue 178 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI1 33) chain B residue 178 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI1 34) chain A residue 63 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 35) chain B residue 288 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 36) chain A residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 37) chain A residue 164 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 38) chain A residue 168 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 39) chain A residue 288 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 40) chain B residue 63 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 41) chain B residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 42) chain B residue 164 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 43) chain B residue 168 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI3 44) chain A residue 71 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 71 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 63 type SITE sequence R description Transition state stabilizer => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI5 47) chain B residue 63 type SITE sequence R description Transition state stabilizer => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H source Swiss-Prot : SWS_FT_FI5 48) chain A residue 21 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 24 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 116 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 21 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 24 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 116 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 source Swiss-Prot : SWS_FT_FI2

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