eF-site ID 1dgg-C PDB Code 1dgg Chain C click to enlarge Title HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX Classification OXIDOREDUCTASE Compound CATALASE Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence C:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN Description Functional site 1) chain C residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 2) chain C residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 3) chain C residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 4) chain C residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 5) chain C residue 61 type sequence M description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 6) chain C residue 65 type sequence D description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 7) chain C residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 8) chain C residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 9) chain C residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 10) chain C residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 11) chain C residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 12) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 13) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 14) chain C residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 15) chain C residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 16) chain C residue 158 type sequence P description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 17) chain C residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 18) chain C residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 19) chain C residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 20) chain C residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 21) chain C residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 22) chain C residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 23) chain C residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 24) chain C residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 25) chain C residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 26) chain C residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 27) chain C residue 194 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 28) chain C residue 198 type sequence F description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 29) chain C residue 201 type sequence S description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 30) chain C residue 203 type sequence R description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 31) chain C residue 213 type sequence N description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 32) chain C residue 235 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 33) chain C residue 237 type sequence K description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 34) chain C residue 303 type sequence W description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 35) chain C residue 304 type sequence P description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 36) chain C residue 305 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 37) chain C residue 442 type sequence Q description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 38) chain C residue 446 type sequence F description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 39) chain C residue 450 type sequence V description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 40) chain C residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 41) chain C residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 42) chain C residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 43) chain C residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 44) chain C residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 45) chain C residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 194 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 48) chain C residue 201 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 49) chain C residue 203 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 50) chain C residue 213 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 51) chain C residue 303 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 52) chain C residue 305 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI2 53) chain C residue 237 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGH source Swiss-Prot : SWS_FT_FI3 54) chain C residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 55) chain C residue 358 type BINDING sequence Y description axial binding residue => ECO:0000269|PubMed:10656833, ECO:0000269|PubMed:10666617, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH, ECO:0007744|PDB:1F4J, ECO:0007744|PDB:1QQW source Swiss-Prot : SWS_FT_FI5 56) chain C residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 57) chain C residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 58) chain C residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7

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