eF-site ID 1yca-AB PDB Code 1yca Chain A, B click to enlarge Title DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY Classification OXYGEN STORAGE Compound MYOGLOBIN Source Sus scrofa (Pig) (MYG_PIG) Sequence A:  GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETL EKFDKFKHLKSEDEMKASEDLKKHGNTTLTALGGILKKKG HHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHP GDFGADAQGAMSKALELFRNDMAAKYKELGFQG B:  GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETL EKFDKFKHLKSEDEMKASEDLKKHGNTTLTALGGILKKKG HHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHP GDFGADAQGAMSKALELFRNDMAAKYKELGFQG Description Functional site 1) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 2) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 3) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 4) chain A residue 67 type sequence T description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 5) chain A residue 68 type sequence T description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 6) chain A residue 71 type sequence A description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 7) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 8) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 9) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 10) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 11) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 12) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 13) chain A residue 107 type sequence I description BINDING SITE FOR RESIDUE HEM A 154 source : AC1 14) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE CMO A 155 source : AC2 15) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE CMO A 155 source : AC2 16) chain A residue 68 type sequence T description BINDING SITE FOR RESIDUE CMO A 155 source : AC2 17) chain B residue 42 type sequence K description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 18) chain B residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 19) chain B residue 64 type sequence H description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 20) chain B residue 68 type sequence T description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 21) chain B residue 71 type sequence A description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 22) chain B residue 89 type sequence L description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 23) chain B residue 92 type sequence S description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 24) chain B residue 93 type sequence H description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 25) chain B residue 97 type sequence H description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 26) chain B residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 27) chain B residue 103 type sequence Y description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 28) chain B residue 138 type sequence F description BINDING SITE FOR RESIDUE HEM B 154 source : AC3 29) chain B residue 43 type sequence F description BINDING SITE FOR RESIDUE CMO B 155 source : AC4 30) chain B residue 64 type sequence H description BINDING SITE FOR RESIDUE CMO B 155 source : AC4 31) chain B residue 68 type sequence T description BINDING SITE FOR RESIDUE CMO B 155 source : AC4 32) chain A residue 4 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 4 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 68 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 68 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04247 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 94 type BINDING sequence A description proximal binding residue => ECO:0000269|PubMed:2383370, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C, ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN, ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI, ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK, ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC, ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG, ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI, ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB, ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB source Swiss-Prot : SWS_FT_FI2 37) chain B residue 94 type BINDING sequence A description proximal binding residue => ECO:0000269|PubMed:2383370, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C, ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN, ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI, ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK, ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC, ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG, ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI, ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB, ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB source Swiss-Prot : SWS_FT_FI2 38) chain A residue 65 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1MNO source Swiss-Prot : SWS_FT_FI1 39) chain B residue 65 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1MNO source Swiss-Prot : SWS_FT_FI1

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