eF-site ID 4coo-B PDB Code 4coo Chain B click to enlarge Title Crystal structure of human cystathionine beta-synthase (delta516-525) at 2.0 angstrom resolution Classification LYASE Compound CYSTATHIONINE BETA-SYNTHASE Source Homo sapiens (Human) (CBS_HUMAN) Sequence B:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKKPWW WHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVV DEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQ IRLTDTLGRLSHILEMDHFALVVHEQQMVFGVVTAIDLLN FVAAQER Description Functional site 1) chain B residue 50 type sequence S description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 2) chain B residue 51 type sequence R description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 3) chain B residue 52 type sequence C description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 4) chain B residue 53 type sequence T description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 5) chain B residue 59 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 6) chain B residue 62 type sequence E description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 7) chain B residue 63 type sequence S description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 8) chain B residue 64 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 9) chain B residue 65 type sequence H description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 10) chain B residue 226 type sequence A description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 11) chain B residue 229 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 12) chain B residue 233 type sequence Y description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 13) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 14) chain B residue 119 type sequence K description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 15) chain B residue 146 type sequence T description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 16) chain B residue 147 type sequence S description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 17) chain B residue 149 type sequence N description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 18) chain B residue 150 type sequence T description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 19) chain B residue 222 type sequence Q description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 20) chain B residue 187 type sequence E description BINDING SITE FOR RESIDUE ACT B 1541 source : AC5 21) chain B residue 189 type sequence V description BINDING SITE FOR RESIDUE ACT B 1541 source : AC5 22) chain B residue 409 type sequence W description BINDING SITE FOR RESIDUE ACT B 1542 source : AC6 23) chain B residue 530 type sequence L description BINDING SITE FOR RESIDUE ACT B 1542 source : AC6 24) chain B residue 119 type sequence K description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 25) chain B residue 149 type sequence N description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 26) chain B residue 254 type sequence S description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 27) chain B residue 255 type sequence V description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 28) chain B residue 256 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 29) chain B residue 257 type sequence T description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 30) chain B residue 258 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 31) chain B residue 259 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 32) chain B residue 260 type sequence T description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 33) chain B residue 304 type sequence E description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 34) chain B residue 305 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 35) chain B residue 306 type sequence I description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 36) chain B residue 349 type sequence S description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 37) chain B residue 375 type sequence P description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 38) chain B residue 376 type sequence D description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 39) chain B residue 50 type sequence S description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 40) chain B residue 262 type sequence T description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 41) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 42) chain B residue 313 type sequence T description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 43) chain B residue 314 type sequence V description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 44) chain B residue 462 type sequence G description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 45) chain B residue 172 type sequence K description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 46) chain B residue 173 type sequence M description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 47) chain B residue 305 type sequence G description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 48) chain B residue 306 type sequence I description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 49) chain B residue 500 type sequence S description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 50) chain B residue 504 type sequence E description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 51) chain B residue 529 type sequence L description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 52) chain B residue 119 type catalytic sequence K description 713 source MCSA : MCSA2 53) chain B residue 52 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 65 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 149 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 256 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 349 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 119 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI4 59) chain B residue 199 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 211 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506 source Swiss-Prot : SWS_FT_FI6

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