eF-site ID 4coo-A PDB Code 4coo Chain A 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 A:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDL TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKG FDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKV IYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQMVFGVVT AIDLLNFVAAQER Description Functional site 1) chain A residue 50 type sequence S description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 2) chain A residue 51 type sequence R description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 3) chain A residue 52 type sequence C description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 4) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 5) chain A residue 54 type sequence W description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 6) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 7) chain A residue 63 type sequence S description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 8) chain A residue 64 type sequence P description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 9) chain A residue 65 type sequence H description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 10) chain A residue 224 type sequence R description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 11) chain A residue 226 type sequence A description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 12) chain A residue 230 type sequence L description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 13) chain A residue 233 type sequence Y description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 14) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE HEM A 1549 source : AC1 15) chain A residue 119 type sequence K description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 16) chain A residue 146 type sequence T description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 17) chain A residue 147 type sequence S description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 18) chain A residue 149 type sequence N description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 19) chain A residue 150 type sequence T description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 20) chain A residue 222 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 21) chain A residue 119 type sequence K description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 22) chain A residue 149 type sequence N description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 23) chain A residue 254 type sequence S description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 24) chain A residue 255 type sequence V description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 25) chain A residue 256 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 26) chain A residue 257 type sequence T description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 27) chain A residue 258 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 28) chain A residue 259 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 29) chain A residue 260 type sequence T description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 30) chain A residue 305 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 31) chain A residue 306 type sequence I description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 32) chain A residue 349 type sequence S description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 33) chain A residue 375 type sequence P description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 34) chain A residue 376 type sequence D description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 35) chain A residue 50 type sequence S description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 36) chain A residue 229 type sequence P description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 37) chain A residue 262 type sequence T description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 38) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 39) chain A residue 313 type sequence T description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 40) chain A residue 314 type sequence V description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 41) chain A residue 195 type sequence A description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 42) chain A residue 197 type sequence F description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 43) chain A residue 202 type sequence S description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 44) chain A residue 203 type sequence H description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 45) chain A residue 308 type sequence Y description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 46) chain A residue 309 type sequence D description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 47) chain A residue 187 type sequence E description BINDING SITE FOR RESIDUE EDO A 1554 source : BC3 48) chain A residue 485 type sequence K description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 49) chain A residue 486 type sequence Q description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 50) chain A residue 487 type sequence F description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 51) chain A residue 315 type sequence L description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 52) chain A residue 316 type sequence D description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 53) chain A residue 317 type sequence R description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 54) chain A residue 198 type sequence D description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 55) chain A residue 200 type sequence P description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 56) chain A residue 436 type sequence E description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 57) chain A residue 439 type sequence R description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 58) chain A residue 172 type sequence K description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 59) chain A residue 173 type sequence M description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 60) chain A residue 305 type sequence G description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 61) chain A residue 306 type sequence I description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 62) chain A residue 188 type sequence I description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 63) chain A residue 189 type sequence V description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 64) chain A residue 539 type sequence L description BINDING SITE FOR RESIDUE EDO A 1559 source : CC1 65) chain A residue 540 type sequence L description BINDING SITE FOR RESIDUE EDO A 1559 source : CC1 66) chain A residue 108-126 type prosite sequence KCEFFNAGGSVKDRISLRM description CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM source prosite : PS00901 67) chain A 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 68) chain A residue 52 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 65 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 149 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 256 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 349 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 73) chain A 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 74) chain A residue 199 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 75) chain A residue 119 type catalytic sequence K description 713 source MCSA : MCSA1

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