eF-site ID 4f4o-ABCDEFGHIJKL PDB Code 4f4o Chain A, B, C, D, E, F, G, H, I, J, K, L Title Structure of the Haptoglobin-Haemoglobin Complex Classification OXYGEN TRANSPORT/TRANSPORT PROTEIN Compound Hemoglobin subunit alpha Source ORGANISM_COMMON: pigs,swine,wild boar; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTK TYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPS VHASLDKFLANVSTVLTSKYR B:  VHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDN LKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGH DFNPNVQAAFQKVVAGVANALAHKYH C:  CPKPPEIPKGYVEHMVRYHCQTYYKLRTAGDGVYTLDSNK QWTNKVTGEKLPECEAVCGKPKNPVIMGGSLDAKGSFPWQ AKMISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKD IAPTLRLYVGKKQEVEIEKVIFHPDNSTVDIGLIKLKQKV PVNERVMPICLPSKDYVNVGLVGYVSGWGRNANLNFTEHL KYVMLPVADQEKCVQYYEGSTVPEKKTPKSPVGVQPILNE HTFCAGLSKYQEDTCYGDAGSAFAVHDKDDDTWYAAGILS FDKSCRTAEYGVYVRVTSILDWIQTTIAD D:  VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTK TYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPS VHASLDKFLANVSTVLTSKYR E:  VHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDN LKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGH DFNPNVQAAFQKVVAGVANALAHKYH F:  CPKPPEIPKGYVEHMVRYHCQTYYKLRTAGDGVYTLDSNK QWTNKVTGEKLPECEAVCGKPKNPVIMGGSLDAKGSFPWQ AKMISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKD IAPTLRLYVGKKQEVEIEKVIFHPDNSTVDIGLIKLKQKV PVNERVMPICLPSKDYVNVGLVGYVSGWGRNANLNFTEHL KYVMLPVADQEKCVQYYEGSTVPEKKTPKSPVGVQPILNE HTFCAGLSKYQEDTCYGDAGSAFAVHDKDDDTWYAAGILS FDKSCRTAEYGVYVRVTSILDWIQTTIAD G:  VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTK TYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPS VHASLDKFLANVSTVLTSKYR H:  VHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDN LKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGH DFNPNVQAAFQKVVAGVANALAHKYH I:  CPKPPEIPKGYVEHMVRYHCQTYYKLRTAGDGVYTLDSNK QWTNKVTGEKLPECEAVCGKPKNPVIMGGSLDAKGSFPWQ AKMISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKD IAPTLRLYVGKKQEVEIEKVIFHPDNSTVDIGLIKLKQKV PVNERVMPICLPSKDYVNVGLVGYVSGWGRNANLNFTEHL KYVMLPVADQEKCVQYYEGSTVPEKKTPKSPVGVQPILNE HTFCAGLSKYQEDTCYGDAGSAFAVHDKDDDTWYAAGILS FDKSCRTAEYGVYVRVTSILDWIQTTIAD J:  VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTK TYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPS VHASLDKFLANVSTVLTSKYR K:  VHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDN LKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGH DFNPNVQAAFQKVVAGVANALAHKYH L:  CPKPPEIPKGYVEHMVRYHCQTYYKLRTAGDGVYTLDSNK QWTNKVTGEKLPECEAVCGKPKNPVIMGGSLDAKGSFPWQ AKMISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKD IAPTLRLYVGKKQEVEIEKVIFHPDNSTVDIGLIKLKQKV PVNERVMPICLPSKDYVNVGLVGYVSGWGRNANLNFTEHL KYVMLPVADQEKCVQYYEGSTVPEKKTPKSPVGVQPILNE HTFCAGLSKYQEDTCYGDAGSAFAVHDKDDDTWYAAGILS FDKSCRTAEYGVYVRVTSILDWIQTTIAD Description Functional site 1) chain C residue 125 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 2) chain I residue 151 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 3) chain I residue 183 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 4) chain I residue 232 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 5) chain L residue 125 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 6) chain L residue 151 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 7) chain L residue 183 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 8) chain L residue 232 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 9) chain C residue 151 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 10) chain C residue 183 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 11) chain C residue 232 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 12) chain F residue 125 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 13) chain F residue 151 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 14) chain F residue 183 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 15) chain F residue 232 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 16) chain I residue 125 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22922649 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 1 type MOD_RES sequence V description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 18) chain E residue 1 type MOD_RES sequence V description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 19) chain H residue 1 type MOD_RES sequence V description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 20) chain K residue 1 type MOD_RES sequence V description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 21) chain G residue 3 type MOD_RES sequence S description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 22) chain G residue 49 type MOD_RES sequence S description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 23) chain J residue 3 type MOD_RES sequence S description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 24) chain J residue 49 type MOD_RES sequence S description N-acetylvaline => ECO:0000250|UniProtKB:P02086 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 26) chain J residue 7 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 27) chain J residue 11 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 28) chain J residue 40 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 29) chain E residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 30) chain H residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 31) chain K residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 32) chain D residue 11 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 33) chain D residue 40 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 34) chain G residue 7 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 35) chain G residue 11 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 36) chain G residue 40 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 38) chain J residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 39) chain J residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 40) chain J residue 137 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 42) chain A residue 137 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 43) chain D residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 44) chain D residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 45) chain D residue 137 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 46) chain G residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 47) chain G residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 48) chain G residue 137 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI7 49) chain B residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 50) chain K residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 51) chain K residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 52) chain K residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 53) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 54) chain B residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 55) chain E residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 56) chain E residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 57) chain E residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 58) chain H residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 59) chain H residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 60) chain H residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 62) chain J residue 102 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 63) chain J residue 124 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 64) chain J residue 138 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 65) chain E residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 66) chain H residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 67) chain K residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 68) chain D residue 124 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 69) chain D residue 138 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 70) chain G residue 102 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 71) chain G residue 124 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 72) chain G residue 138 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 73) chain B residue 92 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139, ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH, ECO:0007744|PDB:4F4O source Swiss-Prot : SWS_FT_FI2 74) chain E residue 92 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139, ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH, ECO:0007744|PDB:4F4O source Swiss-Prot : SWS_FT_FI2 75) chain H residue 92 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139, ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH, ECO:0007744|PDB:4F4O source Swiss-Prot : SWS_FT_FI2 76) chain K residue 92 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139, ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH, ECO:0007744|PDB:4F4O source Swiss-Prot : SWS_FT_FI2

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