eF-site ID 1dug-AB PDB Code 1dug Chain A, B click to enlarge Title STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION Classification transferase, blood clotting Compound chimera of GLUTATHIONE S-TRANSFERASE-synthetic LINKEr-C-TERMINAL FIBRINOGEN GAMMA CHAIN Source null (FIBG_HUMAN) Sequence A:  SPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKW RNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNM LGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVD FLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDV VLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAW PLQGWQATFGGGDHPPKSDPQQHHLGGAKQAGDV B:  SPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKW RNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNM LGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVD FLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDV VLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAW PLQGWQATFGGGDHPPKSDPQQHHLGGAKQAGDV Description Functional site 1) chain A residue 6 type sequence Y description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 2) chain A residue 7 type sequence W description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 3) chain A residue 12 type sequence L description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 4) chain A residue 40 type sequence W description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 5) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 6) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 7) chain A residue 54 type sequence L description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 8) chain A residue 55 type sequence P description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 9) chain A residue 66 type sequence Q description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 10) chain A residue 67 type sequence S description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 11) chain B residue 100 type sequence D description BINDING SITE FOR RESIDUE GSH A 1239 source : AC1 12) chain A residue 100 type sequence D description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 13) chain B residue 6 type sequence Y description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 14) chain B residue 7 type sequence W description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 15) chain B residue 12 type sequence L description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 16) chain B residue 40 type sequence W description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 17) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 18) chain B residue 53 type sequence N description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 19) chain B residue 54 type sequence L description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 20) chain B residue 55 type sequence P description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 21) chain B residue 66 type sequence Q description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 22) chain B residue 67 type sequence S description BINDING SITE FOR RESIDUE GSH B 1587 source : AC2 23) chain A residue 110 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 110 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 53 type BINDING sequence N description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 66 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 6 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 53 type BINDING sequence N description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 66 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 6 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 229 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI4 34) chain B residue 229 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI4 35) chain A residue 221 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432) source Swiss-Prot : SWS_FT_FI3 36) chain B residue 221 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432) source Swiss-Prot : SWS_FT_FI3

Display surface Download Links