eF-site ID 1ihp-A PDB Code 1ihp Chain A click to enlarge Title STRUCTURE OF PHOSPHOMONOESTERASE Classification PHOSPHOMONOESTERASE Compound PHYTASE Source ORGANISM_SCIENTIFIC: Aspergillus ficuum; Sequence A:  SCDTVDQGYQCFSETSHLWGQYAPFFSLANESVISPEVPA GCRVTFAQVLSRHGARYPTDSKGKKYSALIEEIQQNATTF DGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYES LTRNIVPFIRSSGSSRVIASGKKFIEGFQSTKLKDPRAQP GQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEA NFTATFVPSIRQRLENDLSGVTLTDTEVTYLMDMCSFDTI STTKLSPFCDLFTHDEWINYDYLQSLKKYYGHGAGNPLGP TQGVGYANELIARLTHSPVHDDTSSNHTLDSSPATFPLNS TLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTD GFSSAWTVPFASRLYVEMMQCQAEQEPLVRVLVNDRVVPL HGCPVDALGRCTRDSFVRGLSFARSGGDWAECFA Description (1)  PHYTASE Functional site 1) chain A residue 163 type sequence R description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 2) chain A residue 423 type sequence R description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 3) chain A residue 50-64 type prosite sequence VTFAQVLSRHGARYP description HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. VtfAqvLsRHGaRyP source prosite : PS00616 4) chain A residue 332-348 type prosite sequence LYADFSHDNGIISILFA description HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LyADfSHDNGIisIlfA source prosite : PS00778 5) chain A residue 59 type ACT_SITE sequence H description Nucleophile => ECO:0000269|PubMed:9164457, ECO:0007744|PDB:1IHP source Swiss-Prot : SWS_FT_FI1 6) chain A residue 27 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 7) chain A residue 338 type BINDING sequence H description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 8) chain A residue 339 type BINDING sequence D description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 9) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 10) chain A residue 58 type BINDING sequence R description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 11) chain A residue 59 type BINDING sequence H description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 12) chain A residue 62 type BINDING sequence R description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 13) chain A residue 65 type BINDING sequence T description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 14) chain A residue 142 type BINDING sequence R description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 15) chain A residue 188 type BINDING sequence D description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 16) chain A residue 278 type BINDING sequence K description BINDING => ECO:0000305|PubMed:20541524, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI2 17) chain A residue 82 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4P, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI3 18) chain A residue 316 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4P, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI3 19) chain A residue 353 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4P, ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI3 20) chain A residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:3K4Q source Swiss-Prot : SWS_FT_FI4

Display surface Download Links