eF-site ID 1bbz-ACEG PDB Code 1bbz Chain A, C, E, G click to enlarge Title CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS Classification COMPLEX (TRANSFERASE/PEPTIDE) Compound ABL TYROSINE KINASE Source Homo sapiens (Human) (1BBZ) Sequence A:  NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQ TKNGQGWVPSNYITPVNS C:  NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQ TKNGQGWVPSNYITPVNS E:  NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQ TKNGQGWVPSNYITPVNS G:  NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQ TKNGQGWVPSNYITPVNS Description Functional site 1) chain A residue 31 type sequence N description BINDING SITE FOR RESIDUE SO4 A 3000 source : AC1 2) chain A residue 32 type sequence H description BINDING SITE FOR RESIDUE SO4 A 3000 source : AC1 3) chain C residue 31 type sequence N description BINDING SITE FOR RESIDUE SO4 C 3001 source : AC2 4) chain C residue 32 type sequence H description BINDING SITE FOR RESIDUE SO4 C 3001 source : AC2 5) chain G residue 31 type sequence N description BINDING SITE FOR RESIDUE SO4 G 3002 source : AC3 6) chain G residue 32 type sequence H description BINDING SITE FOR RESIDUE SO4 G 3002 source : AC3 7) chain E residue 31 type sequence N description BINDING SITE FOR RESIDUE SO4 E 3003 source : AC4 8) chain E residue 32 type sequence H description BINDING SITE FOR RESIDUE SO4 E 3003 source : AC4 9) chain A residue 7 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435 source Swiss-Prot : SWS_FT_FI1 10) chain C residue 7 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435 source Swiss-Prot : SWS_FT_FI1 11) chain E residue 7 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435 source Swiss-Prot : SWS_FT_FI1 12) chain G residue 7 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 52 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 52 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI2 15) chain E residue 52 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI2 16) chain G residue 52 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI2

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