eF-site ID 3dzh-AB PDB Code 3dzh Chain A, B click to enlarge Title Crystal structure of human CD38 extracellular domain, GTP complex Classification HYDROLASE Compound ADP-ribosyl cyclase 1 Source Homo sapiens (Human) (CD38_HUMAN) Sequence A:  RWRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQS VWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFD TSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV HVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIH GGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF LQCVKNPEDSSC B:  RWRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQS VWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFD TSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV HVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIH GGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF LQCVKNPEDSSC Description Functional site 1) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 2) chain A residue 145 type sequence L description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 3) chain A residue 146 type sequence E description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 4) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 5) chain A residue 176 type sequence W description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 6) chain A residue 177 type sequence R description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 7) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 8) chain A residue 193 type sequence S description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 9) chain A residue 221 type sequence T description BINDING SITE FOR RESIDUE GTP A 301 source : AC1 10) chain B residue 125 type sequence W description BINDING SITE FOR RESIDUE GTP B 301 source : AC2 11) chain B residue 146 type sequence E description BINDING SITE FOR RESIDUE GTP B 301 source : AC2 12) chain B residue 155 type sequence D description BINDING SITE FOR RESIDUE GTP B 301 source : AC2 13) chain B residue 189 type sequence W description BINDING SITE FOR RESIDUE GTP B 301 source : AC2 14) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE GTP B 301 source : AC2 15) chain A residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 17) 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 18) 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 19) chain A residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links