eF-site ID 2o3s-AB PDB Code 2o3s Chain A, B click to enlarge Title Structural Basis for Formation and Hydrolysis of Calcium Messenger Cyclic ADP-ribose by Human CD38 Classification HYDROLASE Compound ADP-ribosyl cyclase 1 Source Homo sapiens (Human) (CD38_HUMAN) Sequence A:  FWRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQS VWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFD TSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV HVMLDGSRSKIFDKDSTFGSVGVHNLQPEKVQTLEAWVIH GGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF LQCVKNPEDSSC B:  FWRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQS VWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFD TSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV HVMLDGSRSKIFDKDSTFGSVGVHNLQPEKVQTLEAWVIH GGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF LQCVKNPEDSSC Description Functional site 1) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 2) chain A residue 127 type sequence R description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 3) chain A residue 129 type sequence K description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 4) chain A residue 146 type sequence E description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 5) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 6) chain A residue 156 type sequence D description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 7) chain A residue 185 type sequence V description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 8) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 9) chain A residue 221 type sequence T description BINDING SITE FOR RESIDUE CXR A 301 source : AC1 10) chain B residue 125 type sequence W description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 11) chain B residue 127 type sequence R description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 12) chain B residue 129 type sequence K description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 13) chain B residue 146 type sequence E description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 14) chain B residue 155 type sequence D description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 15) chain B residue 156 type sequence D description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 16) chain B residue 185 type sequence V description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 17) chain B residue 189 type sequence W description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 18) chain B residue 193 type sequence S description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 19) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE CXR B 301 source : AC2 20) chain A residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 219 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 219 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI4

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