eF-site ID 5e6x-A PDB Code 5e6x Chain A click to enlarge Title Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit Classification CELL ADHESION Compound Integrin beta-2 Source (ITB2_HUMAN) Sequence A:  QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRC DTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQK VTLYLRPGQAAAFNVTFRRAKLSSRVFLDHNALPDTLKVT YDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECI QEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHG KGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDN NSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCEHHHHHH Description Functional site 1) chain A residue 358 type BINDING sequence V description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72 source Swiss-Prot : SWS_FT_FI2 2) chain A residue 481 type BINDING sequence S description in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI5 3) chain A residue 448-459 type prosite sequence CRCDTGYIGKNC description EGF_1 EGF-like domain signature 1. CrCdtGyiGKnC source prosite : PS00022 4) chain A residue 484-497 type prosite sequence CSGLGDCVCGQCLC description INTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsGl..GdCvCgqClC source prosite : PS00243 5) chain A residue 448-461 type prosite sequence CRCDTGYIGKNCEC description EGF_2 EGF-like domain signature 2. CrCdtGYigknce..C source prosite : PS01186 6) chain A residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816 source Swiss-Prot : SWS_FT_FI7 7) chain A residue 28 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI8 8) chain A residue 94 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI9 9) chain A residue 429 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI10 10) chain A residue 471 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI11 11) chain A residue 353 type BINDING sequence P description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI1 12) chain A residue 355 type BINDING sequence T description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI1 13) chain A residue 451 type BINDING sequence D description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI1 14) chain A residue 359 type BINDING sequence T description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI3 15) chain A residue 390 type BINDING sequence Q description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI4 16) chain A residue 446 type BINDING sequence G description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI4 17) chain A residue 448 type BINDING sequence C description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI4 18) chain A residue 450 type BINDING sequence C description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN source Swiss-Prot : SWS_FT_FI4

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