eF-site ID 1j3f-A PDB Code 1j3f Chain A click to enlarge Title Crystal Structure of an Artificial Metalloprotein:Cr(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin Classification OXYGEN STORAGE/TRANSPORT Compound Myoglobin Source null (MYG_PHYCA) Sequence A:  MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPET LEKFDRFKHLKTEAEMKASEDLKKHGVTVLTGLGAILKKK GHHEAELKPLAQSHATKIPIKYLEFISEAIIHVLHSRHPG DFGADAQGAMNKALELFRKDIAAKYKELGYQG Description Functional site 1) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE CR A 190 source : AC1 2) chain A residue 31 type sequence R description BINDING SITE FOR RESIDUE PO4 A 155 source : AC2 3) chain A residue 80 type sequence G description BINDING SITE FOR RESIDUE PO4 A 155 source : AC2 4) chain A residue 81 type sequence H description BINDING SITE FOR RESIDUE PO4 A 155 source : AC2 5) chain A residue 113 type sequence H description BINDING SITE FOR RESIDUE PO4 A 155 source : AC2 6) chain A residue 0 type sequence M description BINDING SITE FOR RESIDUE PO4 A 156 source : AC3 7) chain A residue 113 type sequence H description BINDING SITE FOR RESIDUE PO4 A 156 source : AC3 8) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE PO4 A 156 source : AC3 9) chain A residue 16 type sequence K description BINDING SITE FOR RESIDUE PO4 A 157 source : AC4 10) chain A residue 119 type sequence H description BINDING SITE FOR RESIDUE PO4 A 157 source : AC4 11) chain A residue 122 type sequence D description BINDING SITE FOR RESIDUE PO4 A 157 source : AC4 12) chain A residue 12 type sequence H description BINDING SITE FOR RESIDUE PO4 A 158 source : AC5 13) chain A residue 16 type sequence K description BINDING SITE FOR RESIDUE PO4 A 158 source : AC5 14) chain A residue 44 type sequence D description BINDING SITE FOR RESIDUE PO4 A 158 source : AC5 15) chain A residue 47 type sequence K description BINDING SITE FOR RESIDUE PO4 A 158 source : AC5 16) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE PO4 A 159 source : AC6 17) chain A residue 83 type sequence E description BINDING SITE FOR RESIDUE PO4 A 159 source : AC6 18) chain A residue 116 type sequence H description BINDING SITE FOR RESIDUE PO4 A 159 source : AC6 19) chain A residue 145 type sequence K description BINDING SITE FOR RESIDUE PO4 A 159 source : AC6 20) chain A residue 148 type sequence E description BINDING SITE FOR RESIDUE PO4 A 159 source : AC6 21) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE PO4 A 160 source : AC7 22) chain A residue 51 type sequence T description BINDING SITE FOR RESIDUE PO4 A 160 source : AC7 23) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE PO4 A 160 source : AC7 24) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 25) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 26) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 27) chain A residue 68 type sequence V description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 28) chain A residue 89 type sequence L description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 29) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 30) chain A residue 99 type sequence I description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 31) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE CZM A 180 source : AC8 32) 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 33) 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 34) chain A residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 source Swiss-Prot : SWS_FT_FI3 35) 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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