eF-site ID 7cat-AB PDB Code 7cat Chain A, B click to enlarge Title The NADPH binding site on beef liver catalase Classification OXIDOREDUCTASE Compound CATALASE Source Bos taurus (Bovine) (CATA_BOVIN) Sequence A:  NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLT VGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFG YFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSA DTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPS FIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDR GIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIK NLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQV MTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPV NYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHR HRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPN YYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQV RTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFS DVHPEYGSRIQALLDKYN B:  NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLT VGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFG YFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSA DTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPS FIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDR GIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIK NLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQV MTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPV NYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHR HRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPN YYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQV RTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFS DVHPEYGSRIQALLDKYN Description Functional site 1) chain A residue 71 type sequence R description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 2) chain A residue 72 type sequence V description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 3) chain A residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 4) chain A residue 74 type sequence H description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 5) chain A residue 111 type sequence R description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 6) chain A residue 130 type sequence G description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 7) chain A residue 145 type sequence V description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 8) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 9) chain A residue 147 type sequence N description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 10) chain A residue 157 type sequence A description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 11) chain A residue 160 type sequence F description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 12) chain A residue 298 type sequence L description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 13) chain A residue 333 type sequence F description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 14) chain A residue 349 type sequence M description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 15) chain A residue 353 type sequence R description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 16) chain A residue 356 type sequence A description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 17) chain A residue 357 type sequence Y description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 18) chain A residue 360 type sequence T description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 19) chain A residue 361 type sequence H description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 20) chain A residue 364 type sequence R description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 21) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 22) chain A residue 193 type sequence H description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 23) chain A residue 197 type sequence F description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 24) chain A residue 200 type sequence S description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 25) chain A residue 202 type sequence R description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 26) chain A residue 234 type sequence H description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 27) chain A residue 236 type sequence K description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 28) chain A residue 241 type sequence I description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 29) chain A residue 301 type sequence V description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 30) chain A residue 302 type sequence W description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 31) chain A residue 303 type sequence P description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 32) chain A residue 304 type sequence H description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 33) chain A residue 441 type sequence Q description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 34) chain A residue 444 type sequence T description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 35) chain A residue 445 type sequence F description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 36) chain A residue 449 type sequence V description BINDING SITE FOR RESIDUE NDP A 508 source : AC2 37) chain A residue 64 type sequence D description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 38) chain B residue 71 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 39) chain B residue 72 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 40) chain B residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 41) chain B residue 74 type sequence H description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 42) chain B residue 111 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 43) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 44) chain B residue 145 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 45) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 46) chain B residue 147 type sequence N description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 47) chain B residue 157 type sequence A description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 48) chain B residue 160 type sequence F description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 49) chain B residue 298 type sequence L description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 50) chain B residue 333 type sequence F description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 51) chain B residue 349 type sequence M description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 52) chain B residue 353 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 53) chain B residue 356 type sequence A description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 54) chain B residue 357 type sequence Y description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 55) chain B residue 360 type sequence T description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 56) chain B residue 361 type sequence H description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 57) chain B residue 364 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 58) chain B residue 193 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 59) chain B residue 197 type sequence F description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 60) chain B residue 200 type sequence S description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 61) chain B residue 202 type sequence R description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 62) chain B residue 234 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 63) chain B residue 236 type sequence K description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 64) chain B residue 241 type sequence I description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 65) chain B residue 301 type sequence V description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 66) chain B residue 302 type sequence W description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 67) chain B residue 303 type sequence P description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 68) chain B residue 304 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 69) chain B residue 441 type sequence Q description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 70) chain B residue 444 type sequence T description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 71) chain B residue 445 type sequence F description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 72) chain B residue 449 type sequence V description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 73) chain A residue 417 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 74) chain A residue 434 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 75) chain B residue 417 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 76) chain B residue 434 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 77) chain A residue 449 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 78) chain A residue 480 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 79) chain B residue 449 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 80) chain B residue 480 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 81) chain A residue 13 type MOD_RES sequence H description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 82) chain A residue 221 type MOD_RES sequence L description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 83) chain B residue 13 type MOD_RES sequence H description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 84) chain B residue 221 type MOD_RES sequence L description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 85) chain A residue 233 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 86) chain A residue 499 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 87) chain B residue 233 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 88) chain B residue 499 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 89) chain A residue 353-361 type prosite sequence RLFAYPDTH description CATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH source prosite : PS00437 90) chain A residue 63-79 type prosite sequence FDRERIPERVVHAKGAG description CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG source prosite : PS00438 91) chain A residue 75 type ACT_SITE sequence A description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661 source Swiss-Prot : SWS_FT_FI1 92) chain B residue 75 type ACT_SITE sequence A description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661 source Swiss-Prot : SWS_FT_FI1 93) chain A residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI2 94) chain B residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 96) chain A residue 203 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 97) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 98) chain A residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 99) chain A residue 303 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 100) chain A residue 305 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 101) chain A residue 442 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 102) chain A residue 445 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 103) chain A residue 446 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 104) chain B residue 194 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 105) chain B residue 198 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 106) chain B residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 107) chain B residue 203 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 108) chain B residue 215 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 109) chain B residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 110) chain B residue 303 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 111) chain B residue 305 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 112) chain B residue 442 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 113) chain B residue 445 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 114) chain B residue 446 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 115) chain A residue 194 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 116) chain A residue 198 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 117) chain A residue 213 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P04040 source Swiss-Prot : SWS_FT_FI4 118) chain B residue 213 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P04040 source Swiss-Prot : SWS_FT_FI4 119) chain A residue 358 type BINDING sequence P description axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI5 120) chain B residue 358 type BINDING sequence P description axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI5 121) chain A residue 9 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P04040 source Swiss-Prot : SWS_FT_FI7 122) chain B residue 9 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P04040 source Swiss-Prot : SWS_FT_FI7

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