eF-site ID 4edz-A PDB Code 4edz Chain A click to enlarge Title Crystal structure of hH-PGDS with water displacing inhibitor Classification Isomerase/Isomerase inhibitor Compound Hematopoietic prostaglandin D synthase Source Homo sapiens (Human) (HPGDS_HUMAN) Sequence A:  PNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPE IKSTLPFGKIPILEVDGLTLHQSLAIARYLTKNTDLAGNT EMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELLT YNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLL VFKPDLLDNHPRLVTLRKKVQAIPAVANWIKRRPQTKL Description Functional site 1) chain A residue 8 type sequence Y description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 2) chain A residue 14 type sequence R description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 3) chain A residue 39 type sequence W description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 4) chain A residue 43 type sequence K description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 5) chain A residue 50 type sequence K description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 6) chain A residue 51 type sequence I description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 7) chain A residue 52 type sequence P description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 8) chain A residue 63 type sequence Q description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 9) chain A residue 64 type sequence S description BINDING SITE FOR RESIDUE GSH A 201 source : AC1 10) chain A residue 11 type sequence M description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 11) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 12) chain A residue 14 type sequence R description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 13) chain A residue 36 type sequence Q description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 14) chain A residue 96 type sequence D description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 15) chain A residue 99 type sequence M description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 16) chain A residue 104 type sequence W description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 17) chain A residue 152 type sequence Y description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 18) chain A residue 155 type sequence I description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 19) chain A residue 199 type sequence L description BINDING SITE FOR RESIDUE 0O5 A 202 source : AC2 20) chain A residue 97 type sequence D description BINDING SITE FOR RESIDUE GSH B 202 source : AC4 21) chain A residue 8 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 14 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 39 type BINDING sequence W description BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 49 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 63 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 source Swiss-Prot : SWS_FT_FI1

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