eF-site ID 7cat-B PDB Code 7cat Chain B click to enlarge Title The NADPH binding site on beef liver catalase Classification OXIDOREDUCTASE Compound CATALASE Source Bos taurus (Bovine) (CATA_BOVIN) Sequence B:  NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLT VGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFG YFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSA DTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPS FIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDR GIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIK NLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQV MTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPV NYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHR HRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPN YYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQV RTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFS DVHPEYGSRIQALLDKYN Description Functional site 1) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE HEM A 507 source : AC1 2) chain B residue 71 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 3) chain B residue 72 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 4) chain B residue 73 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 5) chain B residue 74 type sequence H description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 6) chain B residue 111 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 7) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 8) chain B residue 145 type sequence V description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 9) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 10) chain B residue 147 type sequence N description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 11) chain B residue 157 type sequence A description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 12) chain B residue 160 type sequence F description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 13) chain B residue 298 type sequence L description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 14) chain B residue 333 type sequence F description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 15) chain B residue 349 type sequence M description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 16) chain B residue 353 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 17) chain B residue 356 type sequence A description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 18) chain B residue 357 type sequence Y description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 19) chain B residue 360 type sequence T description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 20) chain B residue 361 type sequence H description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 21) chain B residue 364 type sequence R description BINDING SITE FOR RESIDUE HEM B 507 source : AC3 22) chain B residue 193 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 23) chain B residue 197 type sequence F description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 24) chain B residue 200 type sequence S description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 25) chain B residue 202 type sequence R description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 26) chain B residue 234 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 27) chain B residue 236 type sequence K description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 28) chain B residue 241 type sequence I description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 29) chain B residue 301 type sequence V description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 30) chain B residue 302 type sequence W description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 31) chain B residue 303 type sequence P description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 32) chain B residue 304 type sequence H description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 33) chain B residue 441 type sequence Q description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 34) chain B residue 444 type sequence T description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 35) chain B residue 445 type sequence F description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 36) chain B residue 449 type sequence V description BINDING SITE FOR RESIDUE NDP B 508 source : AC4 37) chain B residue 417 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 38) chain B residue 434 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI10 39) chain B residue 449 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 40) chain B residue 480 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI11 41) chain B residue 13 type MOD_RES sequence H description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 42) chain B residue 221 type MOD_RES sequence L description N6-succinyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI8 43) chain B residue 233 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 44) chain B residue 499 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P24270 source Swiss-Prot : SWS_FT_FI9 45) 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 46) chain B residue 148 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 194 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 48) chain B residue 198 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 49) chain B residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 50) chain B residue 203 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 51) chain B residue 215 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 52) chain B residue 237 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 53) chain B residue 303 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 54) chain B residue 305 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 55) chain B residue 442 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 56) chain B residue 445 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 57) chain B residue 446 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC source Swiss-Prot : SWS_FT_FI3 58) chain B residue 213 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P04040 source Swiss-Prot : SWS_FT_FI4 59) 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 60) 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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