eF-site ID 3kgg-A PDB Code 3kgg Chain A click to enlarge Title X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction Classification HYDROLASE Compound Diisopropyl-fluorophosphatase Source Loligo vulgaris (Common European squid) (DFPA_LOLVU) Sequence A:  EIPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVN GKPAGEILRIDLKTGKKTVICKPEVNGYGGIPAGCQCDRD ANQLFVADMRLGLLVVQTDGTFEEIAKKDSEGRRMQGCND CAFDYEGNLWITAPAGEVAPADYTRSMQEKFGSIYCFTTD GQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKLW SYDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLV ANWGSSHIEVFGPDGGQPKMRIRCPFEKPSNLHFKPQTKT IFVTEHENNAVWKFEWQRNGKKQYCETLKFGIF Description Functional site 1) chain A residue 21 type sequence E description BINDING SITE FOR RESIDUE CA A 500 source : AC1 2) chain A residue 120 type sequence N description BINDING SITE FOR RESIDUE CA A 500 source : AC1 3) chain A residue 175 type sequence N description BINDING SITE FOR RESIDUE CA A 500 source : AC1 4) chain A residue 229 type sequence D description BINDING SITE FOR RESIDUE CA A 500 source : AC1 5) chain A residue 232 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC2 6) chain A residue 273 type sequence L description BINDING SITE FOR RESIDUE CA A 501 source : AC2 7) chain A residue 274 type sequence H description BINDING SITE FOR RESIDUE CA A 501 source : AC2 8) chain A residue 21 type catalytic sequence E description 686 source MCSA : MCSA1 9) chain A residue 37 type catalytic sequence E description 686 source MCSA : MCSA1 10) chain A residue 120 type catalytic sequence N description 686 source MCSA : MCSA1 11) chain A residue 175 type catalytic sequence N description 686 source MCSA : MCSA1 12) chain A residue 229 type catalytic sequence D description 686 source MCSA : MCSA1 13) chain A residue 287 type catalytic sequence H description 686 source MCSA : MCSA1 14) chain A residue 287 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:15966726 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 21 type BINDING sequence E description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 120 type BINDING sequence N description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 175 type BINDING sequence N description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 229 type BINDING sequence D description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 232 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 273 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 274 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 source Swiss-Prot : SWS_FT_FI3

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