eF-site ID 1ak0-A PDB Code 1ak0 Chain A click to enlarge Title P1 NUCLEASE IN COMPLEX WITH A SUBSTRATE ANALOG Classification ENDONUCLEASE Compound P1 NUCLEASE Source ORGANISM_SCIENTIFIC: Penicillium citrinum; Sequence A:  WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASI ASWADEYRLTSAGKWSASLHFIDAEDNPPTNCNVDYERDC GSSGCSISAIANYTQRVSDSSLSSENHAEALRFLVHFIGD MTQPLHDEAYAVGGNKINVTFDGYHDNLHSDWDTYMPQKL IGGHALSDAESWAKTLVQNIESGNYTAQAIGWIKGDNISE PITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDS VIDTIELQIAKGGYRLANWINEIH Description (1)  P1 NUCLEASE, ADENOSINE-5'-(DITHIO)PHOSPHATE, THYMIDINE-5'-(DITHIO)PHOSPHATE Functional site 1) chain A residue 1 type catalytic sequence W description 395 source MCSA : MCSA1 2) chain A residue 153 type catalytic sequence D description 395 source MCSA : MCSA1 3) chain A residue 6 type catalytic sequence H description 395 source MCSA : MCSA1 4) chain A residue 45 type catalytic sequence D description 395 source MCSA : MCSA1 5) chain A residue 48 type catalytic sequence R description 395 source MCSA : MCSA1 6) chain A residue 60 type catalytic sequence H description 395 source MCSA : MCSA1 7) chain A residue 116 type catalytic sequence H description 395 source MCSA : MCSA1 8) chain A residue 120 type catalytic sequence D description 395 source MCSA : MCSA1 9) chain A residue 126 type catalytic sequence H description 395 source MCSA : MCSA1 10) chain A residue 149 type catalytic sequence H description 395 source MCSA : MCSA1 11) chain A residue 1 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 153 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 6 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 15 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 60 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 73 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 116 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 120 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 126 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 149 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 45 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q9C9G4 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 45 type SITE sequence D description Important for catalytic activity => ECO:0000250|UniProtKB:P24021 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 48 type SITE sequence R description Important for catalytic activity => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 138 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 197 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI6

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