eF-site ID 1qwo-A PDB Code 1qwo Chain A click to enlarge Title Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway Classification HYDROLASE Compound phytase Source Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) (PHYA_ASPFU) Sequence A:  CDTVDLGYQCSPATSHLWGQYSPFFSLEDELSVSSKLPKD CRITLVQVLSRXGARYPTSSKSKKYKKLVTAIQANATDFK GKFAFLKTYNYTLGADDLTPFGEQQLVNSGIKFYQRYKAL ARSVVPFIRASGSDRVIASGEKFIEGFQQAKLADPGATNR AAPAISVIIPESETFNNTLDHGVCTKFEASQLGDEVAANF TALFAPDIRARAEKHLPGVTLTDEDVVSLMDMCSFDTVAR TSDASQLSPFCQLFTHNEWKKYNYLQSLGKYYGYGAGNPL GPAQGIGFTNELIARLTRSPVQDHTSTNSTLVSNPATFPL NATMYVDFSHDNSMVSIFFALGLYNGTEPLSRTSVESAKE LDGYSASWVVPFGARAYFETMQCKSEKEPLVRALINDRVV PLHGCDVDKLGRCKLNDFVKGLSWARSGGNWGECF Description (1)  Phytase (E.C.3.1.3.8) Functional site 1) chain A residue 82 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P34752 source Swiss-Prot : SWS_FT_FI4 2) chain A residue 88 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P34752 source Swiss-Prot : SWS_FT_FI4 3) chain A residue 211 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P34752 source Swiss-Prot : SWS_FT_FI4 4) chain A residue 50-64 type prosite sequence ITLVQVLSRXGARYP description HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. ItlVqvLsRHGaRyP source prosite : PS00616 5) chain A residue 332-348 type prosite sequence MYVDFSHDNSMVSIFFA description HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. MyVDfSHDNSMvsIffA source prosite : PS00778 6) chain A residue 105 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0000269|PubMed:15341723, ECO:0007744|PDB:1QWO, ECO:0007744|PDB:1SKB source Swiss-Prot : SWS_FT_FI5 7) chain A residue 207 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0000269|PubMed:15341723, ECO:0007744|PDB:1QWO, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9, ECO:0007744|PDB:1SKA, ECO:0007744|PDB:1SKB source Swiss-Prot : SWS_FT_FI6 8) chain A residue 230 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0000269|PubMed:15341723, ECO:0007744|PDB:1QWO, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9, ECO:0007744|PDB:1SKA, ECO:0007744|PDB:1SKB source Swiss-Prot : SWS_FT_FI6 9) chain A residue 339 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0000269|PubMed:15341723, ECO:0007744|PDB:1QWO, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9, ECO:0007744|PDB:1SKA, ECO:0007744|PDB:1SKB source Swiss-Prot : SWS_FT_FI6 10) chain A residue 376 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0000269|PubMed:15341723, ECO:0007744|PDB:1QWO, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9, ECO:0007744|PDB:1SKA, ECO:0007744|PDB:1SKB source Swiss-Prot : SWS_FT_FI6 11) chain A residue 352 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15136045, ECO:0007744|PDB:1QWO source Swiss-Prot : SWS_FT_FI7 12) chain A residue 82 type ACT_SITE sequence N description Nucleophile => ECO:0000269|PubMed:15136045, ECO:0007744|PDB:1QWO source Swiss-Prot : SWS_FT_FI1 13) chain A residue 50 type BINDING sequence I description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 51 type BINDING sequence T description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 301 type BINDING sequence I description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 81 type BINDING sequence A description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 85 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 165 type BINDING sequence T description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 361 type BINDING sequence T description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 362 type BINDING sequence S description BINDING => ECO:0000305|PubMed:15341723, ECO:0007744|PDB:1SK8, ECO:0007744|PDB:1SK9 source Swiss-Prot : SWS_FT_FI3

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