eF-site ID 3ofs-ABCDEF PDB Code 3ofs Chain A, B, C, D, E, F click to enlarge Title Dynamic conformations of the CD38-mediated NAD cyclization captured using multi-copy crystallography Classification HYDROLASE Compound ADP-ribosyl cyclase 1 Source Homo sapiens (Human) (CD38_HUMAN) Sequence A:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVQRDMFTLADTLLGYLADDLTWCGEFDT SKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVH VMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHG EDSRDLCQDPTIKELESIISKRNIQFSCKNIYRP B:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVQRDMFTLADTLLGYLADDLTWCGEFDT SKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVH VMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHG EDSRDLCQDPTIKELESIISKRNIQFSCKNIYRP C:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVQRDMFTLADTLLGYLADDLTWCGEFDT SKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVH VMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHG GREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRP D:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVQRDMFTLADTLLGYLADDLTWCGEFDT SKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVH VMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHG GDSRDLCQDPTIKELESIISKRNIQFSCKNIYR E:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVQRDMFTLADTLLGYLADDLTWCGEFDT SKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVH VMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHG GREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRP F:  WRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSV WDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILLW SRIKDLAHQFTQVDMFTLADTLLGYLADDLTWCGEFDTSK INYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVM LDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGR EDSRDLCQDPTIKELESIISKRNIQFSCKNIYR Description Functional site 1) chain A residue 124 type sequence L description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 2) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 3) chain A residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 4) chain A residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 5) chain A residue 129 type sequence K description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 6) chain A residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 7) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 8) chain A residue 156 type sequence D description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 9) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 10) chain A residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 11) chain A residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 12) chain A residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 13) chain A residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 14) chain A residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU A 301 source : AC1 15) chain B residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 16) chain B residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 17) chain B residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 18) chain B residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 19) chain B residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 20) chain B residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 21) chain B residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 22) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 23) chain B residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 24) chain B residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU B 301 source : AC2 25) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 26) chain C residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 27) chain C residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 28) chain C residue 129 type sequence K description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 29) chain C residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 30) chain C residue 155 type sequence D description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 31) chain C residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 32) chain C residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 33) chain C residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 34) chain C residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 35) chain C residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 36) chain C residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU C 301 source : AC3 37) chain D residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 38) chain D residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 39) chain D residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 40) chain D residue 129 type sequence K description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 41) chain D residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 42) chain D residue 155 type sequence D description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 43) chain D residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 44) chain D residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 45) chain D residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 46) chain D residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 47) chain D residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 48) chain D residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU D 301 source : AC4 49) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 50) chain E residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 51) chain E residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 52) chain E residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 53) chain E residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 54) chain E residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 55) chain E residue 196 type sequence F description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 56) chain E residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 57) chain E residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 58) chain E residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 59) chain E residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU E 301 source : AC5 60) chain F residue 124 type sequence L description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 61) chain F residue 125 type sequence W description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 62) chain F residue 126 type sequence S description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 63) chain F residue 127 type sequence R description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 64) chain F residue 129 type sequence K description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 65) chain F residue 145 type sequence L description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 66) chain F residue 189 type sequence W description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 67) chain F residue 193 type sequence S description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 68) chain F residue 220 type sequence S description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 69) chain F residue 221 type sequence T description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 70) chain F residue 222 type sequence F description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 71) chain F residue 226 type sequence E description BINDING SITE FOR RESIDUE AVU F 301 source : AC6 72) chain A residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 73) chain B residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 74) chain C residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 75) chain D residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 76) chain E residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 77) chain F residue 164 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 78) 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 79) 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 80) chain C 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 81) chain D 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 82) chain E 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 83) chain F 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 84) chain A residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 85) chain A residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 86) chain B residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 87) chain B residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 88) chain C residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 89) chain C residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 90) chain D residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 91) chain D residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 92) chain E residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 93) chain E residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 94) chain F residue 119 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 95) chain F residue 201 type ACT_SITE sequence C description ACT_SITE => ECO:0000305|PubMed:7961800 source Swiss-Prot : SWS_FT_FI1 96) chain A residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 97) chain A residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 100) chain C residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 101) chain C residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 102) chain D residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 103) chain D residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 104) chain E residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 105) chain E residue 209 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 106) chain F residue 100 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 107) chain F 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