eF-site ID 1dgg-ABCD PDB Code 1dgg Chain A, B, C, D click to enlarge Title HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX Classification OXIDOREDUCTASE Compound CATALASE Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN B:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN C:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN D:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN Description Functional site 1) chain A residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN A 4000 source : AC1 2) chain A residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN A 4000 source : AC1 3) chain A residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN A 4000 source : AC1 4) chain A residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN A 4000 source : AC1 5) chain B residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN B 4001 source : AC2 6) chain B residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN B 4001 source : AC2 7) chain B residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN B 4001 source : AC2 8) chain B residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN B 4001 source : AC2 9) chain C residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 10) chain C residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 11) chain C residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 12) chain C residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN C 4002 source : AC3 13) chain D residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 14) chain D residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 15) chain D residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 16) chain D residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 17) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 18) chain A residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 19) chain A residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 20) chain A residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 21) chain A residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 22) chain A residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 23) chain A residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 24) chain A residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 25) chain A residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 26) chain A residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 27) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 28) chain A residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 29) chain A residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 30) chain A residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 31) chain A residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 32) chain A residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 33) chain A residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 34) chain A residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 35) chain A residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 36) chain C residue 61 type sequence M description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 37) chain C residue 65 type sequence D description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 38) chain A residue 194 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 39) chain A residue 198 type sequence F description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 40) chain A residue 201 type sequence S description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 41) chain A residue 203 type sequence R description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 42) chain A residue 213 type sequence N description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 43) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 44) chain A residue 237 type sequence K description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 45) chain A residue 302 type sequence V description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 46) chain A residue 303 type sequence W description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 47) chain A residue 304 type sequence P description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 48) chain A residue 305 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 49) chain A residue 442 type sequence Q description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 50) chain A residue 446 type sequence F description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 51) chain A residue 450 type sequence V description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 52) chain B residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 53) chain B residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 54) chain B residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 55) chain B residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 56) chain B residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 57) chain B residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 58) chain B residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 59) chain B residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 60) chain B residue 158 type sequence P description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 61) chain B residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 62) chain B residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 63) chain B residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 64) chain B residue 299 type sequence L description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 65) chain B residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 66) chain B residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 67) chain B residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 68) chain B residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 69) chain B residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 70) chain B residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM B 2001 source : AC7 71) chain A residue 61 type sequence M description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 72) chain A residue 65 type sequence D description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 73) chain C residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 74) chain C residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 75) chain C residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 76) chain C residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 77) chain C residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 78) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 79) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 80) chain C residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 81) chain C residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 82) chain C residue 158 type sequence P description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 83) chain C residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 84) chain C residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 85) chain C residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 86) chain C residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 87) chain C residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 88) chain C residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 89) chain C residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 90) chain C residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 91) chain C residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 92) chain C residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 93) chain C residue 194 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 94) chain C residue 198 type sequence F description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 95) chain C residue 201 type sequence S description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 96) chain C residue 203 type sequence R description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 97) chain C residue 213 type sequence N description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 98) chain C residue 235 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 99) chain C residue 237 type sequence K description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 100) chain C residue 303 type sequence W description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 101) chain C residue 304 type sequence P description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 102) chain C residue 305 type sequence H description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 103) chain C residue 442 type sequence Q description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 104) chain C residue 446 type sequence F description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 105) chain C residue 450 type sequence V description BINDING SITE FOR RESIDUE NDP C 3001 source : AC9 106) chain B residue 61 type sequence M description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 107) chain B residue 65 type sequence D description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 108) chain D residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 109) chain D residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 110) chain D residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 111) chain D residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 112) chain D residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 113) chain D residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 114) chain D residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 115) chain D residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 116) chain D residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 117) chain D residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 118) chain D residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 119) chain D residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 120) chain D residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 121) chain D residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 122) chain D residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 123) chain D residue 357 type sequence A description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 124) chain D residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 125) chain D residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 126) chain D residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 127) chain D residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 128) chain A residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 129) chain A residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 130) chain B residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 131) chain B residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 132) chain C residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 133) chain C residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 134) chain D residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 135) chain D residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 136) chain A residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 137) chain A residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 138) chain B residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 139) chain B residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 140) chain C residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 141) chain C residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 142) chain D residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 143) chain D residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 144) chain A residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 145) chain B residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 146) chain C residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 147) chain D residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 148) chain A residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 149) chain A residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 152) chain C residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 153) chain C residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 154) chain D residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 155) chain D residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 156) chain A 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 157) chain B 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 158) chain B 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 159) chain B 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 160) 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 161) 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 162) 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 163) 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 164) 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 165) 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 166) chain D 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 167) chain A 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 168) chain D 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 169) chain D 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 170) chain D 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 171) chain D 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 172) chain D 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 173) chain A 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 174) chain A 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 175) chain A 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 176) chain A 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 177) chain B 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 178) chain B 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 179) chain B 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 180) chain A 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 181) chain B 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 182) 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 183) chain D 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 184) chain A residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 185) chain B residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 186) chain C residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 187) chain D residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 188) chain A residue 354-362 type prosite sequence RLFAYPDTH description CATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH source prosite : PS00437 189) chain A residue 64-80 type prosite sequence FDRERIPERVVHAKGAG description CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG source prosite : PS00438 190) chain A 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 191) chain B 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 192) 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 193) chain D 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 194) chain A residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 195) chain A residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 196) chain B residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 197) chain B residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 198) chain C residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 199) chain C residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 200) chain D residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 201) chain D residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 202) chain A residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7 203) chain B residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7 204) chain C residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7 205) chain D residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7

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