eF-site ID 2g1m-A PDB Code 2g1m Chain A click to enlarge Title Cellular Oxygen Sensing: Crystal Structure of Hypoxia-Inducible Factor Prolyl Hydroxylase (PHD2) Classification OXIDOREDUCTASE Compound Egl nine homolog 1 Source null (EGLN1_HUMAN) Sequence A:  LPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVR ALHDTGKFTDGQLVSSKDIRGDKITWIEGKEPGCETIGLL MSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVR HVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQ FADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFD ADERARAKVKY Description Functional site 1) chain A residue 313 type sequence H description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 2) chain A residue 315 type sequence D description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 3) chain A residue 374 type sequence H description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 4) chain A residue 254 type sequence D description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 5) chain A residue 299 type sequence M description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 6) chain A residue 303 type sequence Y description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 7) chain A residue 310 type sequence Y description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 8) chain A residue 313 type sequence H description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 9) chain A residue 315 type sequence D description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 10) chain A residue 329 type sequence Y description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 11) chain A residue 343 type sequence L description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 12) chain A residue 374 type sequence H description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 13) chain A residue 376 type sequence V description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 14) chain A residue 383 type sequence R description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 15) chain A residue 398 type sequence R description BINDING SITE FOR RESIDUE 4HG A 701 source : AC2 16) chain A residue 313 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 315 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 374 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 383 type BINDING sequence R description BINDING => ECO:0000305|PubMed:19604478 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 201 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:21601578 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 208 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:21601578 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 302 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:21601578 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 323 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:21601578 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 326 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:21601578 source Swiss-Prot : SWS_FT_FI3

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