eF-site ID 2vdr-ABCHL PDB Code 2vdr Chain A, B, C, H, L click to enlarge Title Integrin AlphaIIbBeta3 Headpiece Bound to a chimeric Fibrinogen Gamma chain peptide, LGGAKQRGDV Classification CELL ADHESION/IMMUNE SYSTEM Compound INTEGRIN ALPHA-IIB Source ORGANISM_COMMON: MOUSE; ORGANISM_SCIENTIFIC: MUS MUSCULUS; Sequence A:  LNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAP RTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVG SQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTE EAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDF SWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPV ADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVA VGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRL RGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADR KLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAI APLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLR SRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAY GANQVAVYRAQP B:  GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDL KENLLKDNCAPESIEFPVSEARVLEDRPLSDKQVTQVSPQ RIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKD DLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMY ISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEE VKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLL VFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTT MDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIP GTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEEL SLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGC PQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSH RCNNGNGTFECGVCR C:  AKQRGDV H:  EVQLQQSGAELVKPGASVKLSCTASGFNIKDTYVHWVKQR PEQGLEWIGRIDPANGYTKYDPKFQGKATITADTSSNTAY LQLSSLTSEDTAVYYCVRPLYDYYAMDYWGQGTSVTVSSA KTTAPSVYPLAPVCTTGSSVTLGCLVKGYFPEPVTLTWNS GSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCN VAHPASSTKVDKKIEPRGP L:  DILMTQSPSSMSVSLGDTVSITCHASQGISSNIGWLQQKP GKSFMGLIYYGTNLVDGVPSRFSGSGSGADYSLTISSLDS EDFADYYCVQYAQLPYTFGGGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL NSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKT STSPIVKSFNRNEC Description (1)  INTEGRIN ALPHA-IIB, INTEGRIN BETA-3, FIBRINOGEN, MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN, MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN Functional site 1) chain C residue 406 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 2) chain A residue 305 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 3) chain A residue 365 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 4) chain A residue 367 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 5) chain A residue 369 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 6) chain A residue 371 type CROSSLNK sequence Y description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 7) chain A residue 373 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 8) chain A residue 426 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 9) chain A residue 428 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 10) chain A residue 430 type CROSSLNK sequence N description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 11) chain A residue 432 type CROSSLNK sequence Y description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 12) chain B residue 220 type CROSSLNK sequence E description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 13) chain A residue 434 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 14) chain A residue 247 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 15) chain A residue 250 type CROSSLNK sequence T description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 16) chain A residue 252 type CROSSLNK sequence E description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 17) chain A residue 297 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 18) chain A residue 299 type CROSSLNK sequence N description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 19) chain A residue 301 type CROSSLNK sequence D description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 20) chain A residue 303 type CROSSLNK sequence R description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424) source Swiss-Prot : SWS_FT_FI1 21) chain L residue 192-198 type prosite sequence YTCEATH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH source prosite : PS00290 22) chain B residue 158 type BINDING sequence D description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU source Swiss-Prot : SWS_FT_FI4 23) chain B residue 215 type BINDING sequence N description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU source Swiss-Prot : SWS_FT_FI4 24) chain B residue 217 type BINDING sequence D description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU source Swiss-Prot : SWS_FT_FI4 25) chain B residue 219 type BINDING sequence P description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU source Swiss-Prot : SWS_FT_FI4 26) chain B residue 251 type BINDING sequence D description in LIMBS binding site => ECO:0007744|PDB:4G1M source Swiss-Prot : SWS_FT_FI5 27) chain B residue 335 type BINDING sequence M description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI6 28) chain B residue 99 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI7 29) chain B residue 320 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI8 30) chain B residue 371 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI8 31) chain B residue 452 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI9 32) chain B residue 126 type BINDING sequence D description in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI3 33) chain B residue 127 type BINDING sequence D description in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE source Swiss-Prot : SWS_FT_FI3 34) chain B residue 123 type BINDING sequence S description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCU source Swiss-Prot : SWS_FT_FI2

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