eF-site ID 2jho-A PDB Code 2jho Chain A click to enlarge Title Cyanomet Sperm Whale Myoglobin at 1.4A resolution Classification OXYGEN TRANSPORT Compound Myoglobin Source ORGANISM_COMMON: Sperm whale; ORGANISM_SCIENTIFIC: Physeter catodon; Sequence A:  VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETL EKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRKDIAAKYKELGYQG Description Functional site 1) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 2) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 3) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 4) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 5) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 6) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 7) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 8) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 9) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 10) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 11) chain A residue 104 type sequence L description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 12) chain A residue 116 type sequence H description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 13) chain A residue 128 type sequence Q description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 14) chain A residue 138 type sequence F description BINDING SITE FOR RESIDUE HEM A1154 source : AC1 15) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE CYN A1155 source : AC2 16) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE CYN A1155 source : AC2 17) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE CYN A1155 source : AC2 18) chain A residue 57 type sequence A description BINDING SITE FOR RESIDUE SO4 A1156 source : AC3 19) chain A residue 58 type sequence S description BINDING SITE FOR RESIDUE SO4 A1156 source : AC3 20) chain A residue 59 type sequence E description BINDING SITE FOR RESIDUE SO4 A1156 source : AC3 21) chain A residue 60 type sequence D description BINDING SITE FOR RESIDUE SO4 A1156 source : AC3 22) chain A residue 8 type sequence Q description BINDING SITE FOR RESIDUE ZN A1157 source : AC4 23) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE ZN A1157 source : AC4 24) chain A residue 36 type sequence H description BINDING SITE FOR RESIDUE ZN A1157 source : AC4 25) chain A residue 38 type sequence E description BINDING SITE FOR RESIDUE ZN A1157 source : AC4 26) chain A residue 36 type sequence H description BINDING SITE FOR RESIDUE ZN A1158 source : AC5 27) 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 28) chain A residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 67 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4 30) 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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