eF-site ID 2mgd-A PDB Code 2mgd Chain A click to enlarge Title HIGH RESOLUTION CRYSTAL STRUCTURES OF FIVE DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN Classification OXYGEN STORAGE Compound MYOGLOBIN Source null (MYG_PHYCA) Sequence A:  MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPET LEKFDRFKHLKTEAEMKASEDLKKLGVTVLTALGAILKKK GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRH PGNFGADAQGAMNKALELFRKDIAAKYKELGYQG Description Functional site 1) chain A residue 3 type sequence S description BINDING SITE FOR RESIDUE SO4 A 156 source : AC1 2) chain A residue 4 type sequence E description BINDING SITE FOR RESIDUE SO4 A 156 source : AC1 3) chain A residue 51 type sequence T description BINDING SITE FOR RESIDUE SO4 A 156 source : AC1 4) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE SO4 A 156 source : AC1 5) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 6) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 7) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 8) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 9) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 10) chain A residue 71 type sequence A description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 11) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 12) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 13) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 14) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 15) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 16) chain A residue 104 type sequence L description BINDING SITE FOR RESIDUE HEM A 154 source : AC2 17) chain A residue 64 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO source Swiss-Prot : SWS_FT_FI1 18) 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 19) chain A residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 20) 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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