eF-site ID 2z6s-A PDB Code 2z6s Chain A click to enlarge Title Crystal structure of the oxy myoglobin free from X-ray-induced photoreduction Classification OXYGEN BINDING Compound Myoglobin Source ORGANISM_COMMON: sperm whale; ORGANISM_SCIENTIFIC: Physeter catodon; Sequence A:  VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETL EKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRKDIAAKYKELGYQ Description Functional site 1) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 2) chain A residue 51 type sequence T description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 3) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 4) chain A residue 119 type sequence H description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 5) chain A residue 120 type sequence P description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 6) chain A residue 121 type sequence G description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 7) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 8) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 9) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 10) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 11) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 12) chain A residue 67 type sequence T description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 13) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 14) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 15) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 16) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 17) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 18) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 19) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 20) chain A residue 138 type sequence F description BINDING SITE FOR RESIDUE HEM A 201 source : AC3 21) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE OXY A 401 source : AC4 22) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE OXY A 401 source : AC4 23) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE OXY A 401 source : AC4 24) chain A residue 67 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 64 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO source Swiss-Prot : SWS_FT_FI1 27) chain A residue 93 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN source Swiss-Prot : SWS_FT_FI2

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