eF-site ID 4coo-AB PDB Code 4coo Chain A, 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 A:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDL TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKG FDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKV IYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQMVFGVVT AIDLLNFVAAQER B:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKKPWW WHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVV DEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQ IRLTDTLGRLSHILEMDHFALVVHEQQMVFGVVTAIDLLN FVAAQER 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 B residue 50 type sequence S description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 16) chain B residue 51 type sequence R description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 17) chain B residue 52 type sequence C description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 18) chain B residue 53 type sequence T description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 19) chain B residue 59 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 20) chain B residue 62 type sequence E description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 21) chain B residue 63 type sequence S description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 22) chain B residue 64 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 23) chain B residue 65 type sequence H description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 24) chain B residue 226 type sequence A description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 25) chain B residue 229 type sequence P description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 26) chain B residue 233 type sequence Y description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 27) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE HEM B 1539 source : AC2 28) chain A residue 119 type sequence K description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 29) chain A residue 146 type sequence T description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 30) chain A residue 147 type sequence S description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 31) chain A residue 149 type sequence N description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 32) chain A residue 150 type sequence T description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 33) chain A residue 222 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1550 source : AC3 34) chain B residue 119 type sequence K description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 35) chain B residue 146 type sequence T description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 36) chain B residue 147 type sequence S description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 37) chain B residue 149 type sequence N description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 38) chain B residue 150 type sequence T description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 39) chain B residue 222 type sequence Q description BINDING SITE FOR RESIDUE ACT B 1540 source : AC4 40) chain B residue 187 type sequence E description BINDING SITE FOR RESIDUE ACT B 1541 source : AC5 41) chain B residue 189 type sequence V description BINDING SITE FOR RESIDUE ACT B 1541 source : AC5 42) chain B residue 409 type sequence W description BINDING SITE FOR RESIDUE ACT B 1542 source : AC6 43) chain B residue 530 type sequence L description BINDING SITE FOR RESIDUE ACT B 1542 source : AC6 44) chain A residue 119 type sequence K description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 45) chain A residue 149 type sequence N description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 46) chain A residue 254 type sequence S description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 47) chain A residue 255 type sequence V description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 48) chain A residue 256 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 49) chain A residue 257 type sequence T description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 50) chain A residue 258 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 51) chain A residue 259 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 52) chain A residue 260 type sequence T description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 53) chain A residue 305 type sequence G description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 54) chain A residue 306 type sequence I description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 55) chain A residue 349 type sequence S description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 56) chain A residue 375 type sequence P description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 57) chain A residue 376 type sequence D description BINDING SITE FOR RESIDUE PLP A 1551 source : AC7 58) chain B residue 119 type sequence K description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 59) chain B residue 149 type sequence N description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 60) chain B residue 254 type sequence S description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 61) chain B residue 255 type sequence V description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 62) chain B residue 256 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 63) chain B residue 257 type sequence T description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 64) chain B residue 258 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 65) chain B residue 259 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 66) chain B residue 260 type sequence T description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 67) chain B residue 304 type sequence E description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 68) chain B residue 305 type sequence G description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 69) chain B residue 306 type sequence I description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 70) chain B residue 349 type sequence S description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 71) chain B residue 375 type sequence P description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 72) chain B residue 376 type sequence D description BINDING SITE FOR RESIDUE PLP B 1543 source : AC8 73) chain A residue 50 type sequence S description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 74) chain A residue 229 type sequence P description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 75) chain A residue 262 type sequence T description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 76) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 77) chain A residue 313 type sequence T description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 78) chain A residue 314 type sequence V description BINDING SITE FOR RESIDUE EDO A 1552 source : AC9 79) chain A residue 195 type sequence A description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 80) chain A residue 197 type sequence F description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 81) chain A residue 202 type sequence S description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 82) chain A residue 203 type sequence H description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 83) chain A residue 308 type sequence Y description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 84) chain A residue 309 type sequence D description BINDING SITE FOR RESIDUE EDO A 1553 source : BC1 85) chain B residue 50 type sequence S description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 86) chain B residue 262 type sequence T description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 87) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 88) chain B residue 313 type sequence T description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 89) chain B residue 314 type sequence V description BINDING SITE FOR RESIDUE EDO B 1544 source : BC2 90) chain A residue 187 type sequence E description BINDING SITE FOR RESIDUE EDO A 1554 source : BC3 91) chain A residue 485 type sequence K description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 92) chain A residue 486 type sequence Q description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 93) chain A residue 487 type sequence F description BINDING SITE FOR RESIDUE EDO A 1555 source : BC4 94) chain A residue 315 type sequence L description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 95) chain A residue 316 type sequence D description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 96) chain A residue 317 type sequence R description BINDING SITE FOR RESIDUE EDO A 1556 source : BC5 97) chain A residue 198 type sequence D description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 98) chain A residue 200 type sequence P description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 99) chain A residue 436 type sequence E description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 100) chain A residue 439 type sequence R description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 101) chain B residue 462 type sequence G description BINDING SITE FOR RESIDUE PE4 A 1557 source : BC6 102) chain A residue 172 type sequence K description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 103) chain A residue 173 type sequence M description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 104) chain A residue 305 type sequence G description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 105) chain A residue 306 type sequence I description BINDING SITE FOR RESIDUE NA A 1558 source : BC7 106) chain B residue 172 type sequence K description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 107) chain B residue 173 type sequence M description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 108) chain B residue 305 type sequence G description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 109) chain B residue 306 type sequence I description BINDING SITE FOR RESIDUE NA B 1545 source : BC8 110) chain A residue 188 type sequence I description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 111) chain A residue 189 type sequence V description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 112) chain B residue 500 type sequence S description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 113) chain B residue 504 type sequence E description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 114) chain B residue 529 type sequence L description BINDING SITE FOR RESIDUE ACT B 1546 source : BC9 115) chain A residue 539 type sequence L description BINDING SITE FOR RESIDUE EDO A 1559 source : CC1 116) chain A residue 540 type sequence L description BINDING SITE FOR RESIDUE EDO A 1559 source : CC1 117) chain A residue 119 type catalytic sequence K description 713 source MCSA : MCSA1 118) chain B residue 119 type catalytic sequence K description 713 source MCSA : MCSA2 119) 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 120) 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 121) 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 122) 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 123) 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 124) chain A residue 149 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 125) chain A residue 256 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 126) chain A residue 349 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 127) chain B residue 149 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 128) chain B residue 256 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 129) chain B residue 349 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 source Swiss-Prot : SWS_FT_FI2 130) 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 131) 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 132) chain A residue 199 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 133) chain B residue 199 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 134) 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 135) 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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