eF-site ID 1dgg-D PDB Code 1dgg Chain D click to enlarge Title HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX Classification OXIDOREDUCTASE Compound CATALASE Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence D:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE VHPDYGSHIQALLDKYN Description Functional site 1) chain D residue 74 type sequence V description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 2) chain D residue 75 type sequence H description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 3) chain D residue 161 type sequence F description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 4) chain D residue 358 type sequence Y description BINDING SITE FOR RESIDUE CYN D 4003 source : AC4 5) chain D residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 6) chain D residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 7) chain D residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 8) chain D residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 9) chain D residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 10) chain D residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 11) chain D residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 12) chain D residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 13) chain D residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 14) chain D residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 15) chain D residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 16) chain D residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 17) chain D residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 18) chain D residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 19) chain D residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 20) chain D residue 357 type sequence A description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 21) chain D residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 22) chain D residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 23) chain D residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 24) chain D residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM D 2003 source : BC1 25) chain D residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 26) chain D residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 27) chain D residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 28) chain D residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 29) chain D residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 30) chain D residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) chain D residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 40) 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 41) chain D residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 42) chain D residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 43) 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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