eF-site ID 1fcs-A PDB Code 1fcs Chain A click to enlarge Title CRYSTAL STRUCTURE OF A DISTAL SITE DOUBLE MUTANT OF SPERM WHALE MYOGLOBIN AT 1.6 ANGSTROMS RESOLUTION Classification OXYGEN TRANSPORT Compound MYOGLOBIN Source Physeter macrocephalus (Sperm whale) (Physeter catodon) (MYG_PHYCA) Sequence A:  MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPET LEKFDRFKHLKTEAEMKASEDLKKVGVRVLTALGAILKKK GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRH PGNFGADAQGAMNKALELFRKDIAAKYKELGYQG Description Functional site 1) chain A residue 3 type sequence S description BINDING SITE FOR RESIDUE SO4 A 157 source : AC1 2) chain A residue 4 type sequence E description BINDING SITE FOR RESIDUE SO4 A 157 source : AC1 3) chain A residue 51 type sequence T description BINDING SITE FOR RESIDUE SO4 A 157 source : AC1 4) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE SO4 A 157 source : AC1 5) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE SO4 A 158 source : AC2 6) chain A residue 63 type sequence K description BINDING SITE FOR RESIDUE SO4 A 158 source : AC2 7) chain A residue 67 type sequence R description BINDING SITE FOR RESIDUE SO4 A 158 source : AC2 8) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 9) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 10) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 11) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 12) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 13) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 14) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 15) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 16) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM A 155 source : AC3 17) chain A residue 4 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 68 type MOD_RES sequence V description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 65 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO source Swiss-Prot : SWS_FT_FI1 20) chain A residue 94 type BINDING sequence A 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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