eF-site ID 1dgg-A PDB Code 1dgg Chain A 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 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 A residue 72 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 6) chain A residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 7) chain A residue 74 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 8) chain A residue 75 type sequence H description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 9) chain A residue 112 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 10) chain A residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 11) chain A residue 146 type sequence V description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 12) chain A residue 147 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 13) chain A residue 148 type sequence N description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 14) chain A residue 161 type sequence F description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 15) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 16) chain A residue 217 type sequence S description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 17) chain A residue 334 type sequence F description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 18) chain A residue 350 type sequence M description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 19) chain A residue 354 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 20) chain A residue 358 type sequence Y description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 21) chain A residue 361 type sequence T description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 22) chain A residue 362 type sequence H description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 23) chain A residue 365 type sequence R description BINDING SITE FOR RESIDUE HEM A 2000 source : AC5 24) chain A residue 194 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 25) chain A residue 198 type sequence F description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 26) chain A residue 201 type sequence S description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 27) chain A residue 203 type sequence R description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 28) chain A residue 213 type sequence N description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 29) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 30) chain A residue 237 type sequence K description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 31) chain A residue 302 type sequence V description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 32) chain A residue 303 type sequence W description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 33) chain A residue 304 type sequence P description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 34) chain A residue 305 type sequence H description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 35) chain A residue 442 type sequence Q description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 36) chain A residue 446 type sequence F description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 37) chain A residue 450 type sequence V description BINDING SITE FOR RESIDUE NDP A 3000 source : AC6 38) chain A residue 61 type sequence M description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 39) chain A residue 65 type sequence D description BINDING SITE FOR RESIDUE HEM C 2002 source : AC8 40) chain A residue 306 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF source Swiss-Prot : SWS_FT_FI4 41) chain A residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 42) chain A residue 499 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 43) chain A residue 306 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 44) chain A residue 480 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 45) chain A residue 417 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 46) 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 47) 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 48) chain A residue 422 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 221 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 354-362 type prosite sequence RLFAYPDTH description CATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH source prosite : PS00437 52) chain A residue 64-80 type prosite sequence FDRERIPERVVHAKGAG description CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG source prosite : PS00438 53) chain A residue 75 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000305|PubMed:10656833 source Swiss-Prot : SWS_FT_FI1 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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

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