eF-site ID 2e2y-A PDB Code 2e2y Chain A click to enlarge Title Crystal Structure of F43W/H64D/V68I Myoglobin Classification OXYGEN STORAGE/TRANSPORT Compound Myoglobin Source (Q0KIY8_PHYCA) Sequence A:  MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPET LEKWDRFKHLKTEAEMKASEDLKKDGVTILTALGAILKKK GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRH PGNFGADAQGAMNKALELFRKDIAAKYKELGYQG Description Functional site 1) chain A residue 87 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1001 source : AC1 2) chain A residue 124 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1001 source : AC1 3) chain A residue 125 type sequence A description BINDING SITE FOR RESIDUE SO4 A 1001 source : AC1 4) chain A residue 126 type sequence D description BINDING SITE FOR RESIDUE SO4 A 1001 source : AC1 5) chain A residue 3 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 6) chain A residue 5 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 7) chain A residue 3 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 8) chain A residue 4 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 9) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 10) chain A residue 51 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 11) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 12) chain A residue 53 type sequence A description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 13) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 14) chain A residue 43 type sequence W description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 15) chain A residue 67 type sequence T description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 16) chain A residue 68 type sequence I description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 17) chain A residue 71 type sequence A description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 18) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 19) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 20) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 21) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 22) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A 154 source : AC4 23) chain A residue 57 type sequence A description BINDING SITE FOR RESIDUE GOL A 600 source : AC5 24) chain A residue 58 type sequence S description BINDING SITE FOR RESIDUE GOL A 600 source : AC5 25) chain A residue 59 type sequence E description BINDING SITE FOR RESIDUE GOL A 600 source : AC5 26) chain A residue 60 type sequence D description BINDING SITE FOR RESIDUE GOL A 600 source : AC5 27) chain A residue 64 type BINDING sequence D 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 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 29) chain A residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 67 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4

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