eF-site ID 4p2x-AB PDB Code 4p2x Chain A, B click to enlarge Title Swapped Dimer of Mycobacterial Adenylyl cyclase Rv1625c: Form 2 Classification LYASE Compound Adenylate cyclase Source (CYA1_MYCTU) Sequence A:  RNIIADKYDEASVLFADIVPALVRFLDRLYSAFDELVDQH GLEKIKGDSYMVVSGVPRPRPDHTQALADFALDMTNVAAQ LKDPRNPVPLRVGLATGPVVAGVVGSRRFFYDVWGDAVNV ASRMESTDSVGQIQVPDEVYERLKDDFVLRERGHINVMRT WYLIGRK B:  ERNIIADKYDEASVLFADIVRFLDRLYSAFDELVDQHGLE KIKVSGDSYMVVSGVPRPRPDHTQALADFALDMTNVAAQL KDRGNPVPLRVGLATGPVVAGVVGSRRFFYDVWGDAVNVA SRMESTVGQIQVPDEVYERLKDDFVLRERGHINVKGKGVM RTWYLIGRKVAA Description Functional site 1) chain A residue 405 type sequence R description binding site for residue SO4 A 501 source : AC1 2) chain B residue 411 type sequence K description binding site for residue SO4 A 501 source : AC1 3) chain B residue 412 type sequence G description binding site for residue SO4 A 501 source : AC1 4) chain B residue 424 type sequence R description binding site for residue SO4 A 501 source : AC1 5) chain B residue 427 type sequence A description binding site for residue SO4 A 501 source : AC1 6) chain A residue 421 type sequence L description binding site for residue PEG A 502 source : AC2 7) chain A residue 422 type sequence I description binding site for residue PEG A 502 source : AC2 8) chain B residue 327 type sequence T description binding site for residue PEG A 502 source : AC2 9) chain A residue 240 type sequence R description binding site for residue PEG A 503 source : AC3 10) chain A residue 247 type sequence Y description binding site for residue PEG A 503 source : AC3 11) chain A residue 248 type sequence D description binding site for residue PEG A 503 source : AC3 12) chain A residue 249 type sequence E description binding site for residue PEG A 503 source : AC3 13) chain A residue 307 type sequence G description binding site for residue PEG A 503 source : AC3 14) chain A residue 311 type sequence P description binding site for residue PEG A 503 source : AC3 15) chain A residue 312 type sequence R description binding site for residue PEG A 503 source : AC3 16) chain A residue 245 type sequence D description binding site for residue MG A 504 source : AC4 17) chain A residue 247 type sequence Y description binding site for residue MG A 504 source : AC4 18) chain A residue 354 type sequence A description binding site for residue MG A 504 source : AC4 19) chain A residue 355 type sequence G description binding site for residue MG A 504 source : AC4 20) chain B residue 291 type sequence G description binding site for residue PEG B 501 source : AC5 21) chain B residue 307 type sequence G description binding site for residue PEG B 501 source : AC5 22) chain B residue 308 type sequence V description binding site for residue PEG B 501 source : AC5 23) chain B residue 309 type sequence P description binding site for residue PEG B 501 source : AC5 24) chain B residue 310 type sequence R description binding site for residue PEG B 501 source : AC5 25) chain B residue 312 type sequence R description binding site for residue PEG B 501 source : AC5 26) chain A residue 395 type sequence R description binding site for residue CL B 503 source : AC6 27) chain B residue 314 type sequence D description binding site for residue CL B 503 source : AC6 28) chain B residue 316 type sequence T description binding site for residue CL B 503 source : AC6 29) chain B residue 317 type sequence Q description binding site for residue CL B 503 source : AC6 30) chain A residue 355-378 type prosite sequence GVVGSRRFFYDVWGDAVNVASRME description GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GsrrffYdVWGDAVNvasrmE source prosite : PS00452 31) chain A residue 256 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11447108 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 300 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11447108 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 256 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11447108 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 300 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11447108 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links