eF-site ID 1pjs-AB PDB Code 1pjs Chain A, B click to enlarge Title The co-crystal structure of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis, in complex with it NAD cofactor Classification TRANSFERASE/OXIDOREDUCTASE/LYASE Compound Siroheme synthase Source Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (CYSG_SALTY) Sequence A:  MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTV NALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAAT DDDTVNQRVSDAAESRRIFCNVVDAPKAASFIMPSIIDRS PLMVAVSXGGTSPVLARLLREKLESLLPQHLGQVARYAGQ LRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAV NATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ QADIVVYDRLVSDDIMNLVRRDADRVFVVPQEEINQILLR EAQKGKRVVRLKGGDPFIFGRGGEELETLCHAGIPFSVVP GITAASGCSAYSGIPLTHRDYAQSVRLVTGELDWENLAAE KQTLVFYMGLNQAATIQEKLIAFGMQADMPVALVENGTSV KQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLNWF SNH B:  MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTV NALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAAT DDDTVNQRVSDAAESRRIFCNVVDAPKAASFIMPSIIDRS PLMVAVSXGGTSPVLARLLREKLESLLPQHLGQVARYAGQ LRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAV NATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ QADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQE EINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHA GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHG GELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQADM PVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGR VVALRDKLNWFSNH Description Functional site 1) chain A residue 260 type sequence R description BINDING SITE FOR RESIDUE PO4 B 507 source : AC1 2) chain A residue 261 type sequence R description BINDING SITE FOR RESIDUE PO4 B 507 source : AC1 3) chain B residue 115 type sequence S description BINDING SITE FOR RESIDUE PO4 B 507 source : AC1 4) chain B residue 137 type sequence R description BINDING SITE FOR RESIDUE PO4 B 507 source : AC1 5) chain B residue 140 type sequence R description BINDING SITE FOR RESIDUE PO4 B 507 source : AC1 6) chain A residue 225 type sequence P description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 7) chain A residue 250 type sequence L description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 8) chain A residue 301 type sequence G description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 9) chain A residue 302 type sequence G description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 10) chain A residue 303 type sequence D description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 11) chain A residue 306 type sequence I description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 12) chain A residue 307 type sequence F description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 13) chain A residue 331 type sequence T description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 14) chain A residue 332 type sequence A description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 15) chain A residue 336 type sequence C description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 16) chain A residue 381 type sequence Y description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 17) chain A residue 382 type sequence M description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 18) chain A residue 408 type sequence V description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 19) chain A residue 410 type sequence N description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 20) chain A residue 411 type sequence G description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 21) chain A residue 436 type sequence P description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 22) chain A residue 437 type sequence A description BINDING SITE FOR RESIDUE SAH A 501 source : AC2 23) chain A residue 19 type sequence G description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 24) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 25) chain A residue 21 type sequence G description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 26) chain A residue 22 type sequence D description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 27) chain A residue 23 type sequence V description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 28) chain A residue 42 type sequence A description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 29) chain A residue 43 type sequence L description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 30) chain A residue 44 type sequence T description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 31) chain A residue 63 type sequence G description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 32) chain A residue 80 type sequence T description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 33) chain A residue 81 type sequence D description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 34) chain A residue 85 type sequence V description BINDING SITE FOR RESIDUE NAD A 502 source : AC3 35) chain B residue 225 type sequence P description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 36) chain B residue 301 type sequence G description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 37) chain B residue 302 type sequence G description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 38) chain B residue 303 type sequence D description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 39) chain B residue 306 type sequence I description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 40) chain B residue 307 type sequence F description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 41) chain B residue 331 type sequence T description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 42) chain B residue 332 type sequence A description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 43) chain B residue 336 type sequence C description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 44) chain B residue 381 type sequence Y description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 45) chain B residue 382 type sequence M description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 46) chain B residue 408 type sequence V description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 47) chain B residue 410 type sequence N description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 48) chain B residue 411 type sequence G description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 49) chain B residue 436 type sequence P description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 50) chain B residue 437 type sequence A description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 51) chain B residue 438 type sequence L description BINDING SITE FOR RESIDUE SAH B 503 source : AC4 52) chain A residue 264 type sequence D description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 53) chain B residue 20 type sequence G description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 54) chain B residue 21 type sequence G description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 55) chain B residue 22 type sequence D description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 56) chain B residue 23 type sequence V description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 57) chain B residue 26 type sequence R description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 58) chain B residue 43 type sequence L description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 59) chain B residue 44 type sequence T description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 60) chain B residue 80 type sequence T description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 61) chain B residue 81 type sequence D description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 62) chain B residue 85 type sequence V description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 63) chain B residue 104 type sequence D description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 64) chain B residue 281 type sequence E description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 65) chain B residue 288 type sequence R description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 66) chain B residue 292 type sequence K description BINDING SITE FOR RESIDUE NAD B 504 source : AC5 67) chain A residue 139 type sequence L description BINDING SITE FOR RESIDUE PGE A 505 source : AC6 68) chain A residue 142 type sequence K description BINDING SITE FOR RESIDUE PGE A 505 source : AC6 69) chain B residue 241 type sequence Q description BINDING SITE FOR RESIDUE PGE A 505 source : AC6 70) chain A residue 146 type sequence L description BINDING SITE FOR RESIDUE PGE A 506 source : AC7 71) chain A residue 151 type sequence L description BINDING SITE FOR RESIDUE PGE A 506 source : AC7 72) chain B residue 139 type sequence L description BINDING SITE FOR RESIDUE PGE A 506 source : AC7 73) chain A residue 248 type catalytic sequence D description 702 source MCSA : MCSA1 74) chain A residue 382 type catalytic sequence M description 702 source MCSA : MCSA1 75) chain B residue 248 type catalytic sequence D description 702 source MCSA : MCSA2 76) chain B residue 270 type catalytic sequence K description 702 source MCSA : MCSA2 77) chain B residue 382 type catalytic sequence M description 702 source MCSA : MCSA2 78) chain A residue 248 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI1 79) chain B residue 248 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI1 80) chain B residue 270 type ACT_SITE sequence K description Proton donor => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI2 81) chain A residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 82) chain B residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 83) chain B residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 84) chain B residue 225 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 85) chain B residue 301 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 86) chain B residue 306 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 87) chain B residue 331 type BINDING sequence T description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 88) chain B residue 382 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 411 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 90) chain B residue 437 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 91) chain A residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 92) chain A residue 225 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 93) chain A residue 301 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 94) chain A residue 306 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 95) chain A residue 331 type BINDING sequence T description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 96) chain A residue 382 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 97) chain A residue 411 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 98) chain A residue 437 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI3 99) chain A residue 128 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI4 100) chain B residue 128 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:14595395 source Swiss-Prot : SWS_FT_FI4 101) chain A residue 221-235 type prosite sequence VGAGPGDAGLLTLKG description SUMT_1 Uroporphyrin-III C-methyltransferase signature 1. VGAGPGdagLLTLKG source prosite : PS00839 102) chain A residue 296-329 type prosite sequence VVRLKGGDPFIFGRGGEELETLCHAGIPFSVVPG description SUMT_2 Uroporphyrin-III C-methyltransferase signature 2. VvrLkgGDpfiFGrggeeletLchagipFsVvPG source prosite : PS00840

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