eF-site ID 4r0o-ABCD PDB Code 4r0o Chain A, B, C, D click to enlarge Title Crystal structure of PEGylated plastocyanin at 4.2 A resolution Classification ELECTRON TRANSPORT Compound Plastocyanin Source Phormidium laminosum (PLAS_PHOLA) Sequence A:  METFTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPH NILFDCKQVPGASKELADKLSHSQLMFSPGESYEITFSSD FPAGTYTYYCAPHRGAGMVGKITVEG B:  METFTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPH NILFDCKQVPGASKELADKLSHSQLMFSPGESYEITFSSD FPAGTYTYYCAPHRGAGMVGKITVEG C:  METFTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPH NILFDCKQVPGASKELADKLSHSQLMFSPGESYEITFSSD FPAGTYTYYCAPHRGAGMVGKITVEG D:  METFTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPH NILFDCKQVPGASKELADKLSHSQLMFSPGESYEITFSSD FPAGTYTYYCAPHRGAGMVGKITVEG Description Functional site 1) chain A residue 39 type sequence H description BINDING SITE FOR RESIDUE CU A 201 source : AC1 2) chain A residue 89 type sequence C description BINDING SITE FOR RESIDUE CU A 201 source : AC1 3) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE CU A 201 source : AC1 4) chain A residue 97 type sequence M description BINDING SITE FOR RESIDUE CU A 201 source : AC1 5) chain A residue 44 type sequence D description BINDING SITE FOR RESIDUE LCY A 202 source : AC2 6) chain A residue 45 type sequence C description BINDING SITE FOR RESIDUE LCY A 202 source : AC2 7) chain B residue 39 type sequence H description BINDING SITE FOR RESIDUE CU B 201 source : AC3 8) chain B residue 89 type sequence C description BINDING SITE FOR RESIDUE CU B 201 source : AC3 9) chain B residue 92 type sequence H description BINDING SITE FOR RESIDUE CU B 201 source : AC3 10) chain B residue 97 type sequence M description BINDING SITE FOR RESIDUE CU B 201 source : AC3 11) chain B residue 45 type sequence C description BINDING SITE FOR RESIDUE LCY B 202 source : AC4 12) chain C residue 39 type sequence H description BINDING SITE FOR RESIDUE CU C 201 source : AC5 13) chain C residue 89 type sequence C description BINDING SITE FOR RESIDUE CU C 201 source : AC5 14) chain C residue 92 type sequence H description BINDING SITE FOR RESIDUE CU C 201 source : AC5 15) chain C residue 97 type sequence M description BINDING SITE FOR RESIDUE CU C 201 source : AC5 16) chain C residue 45 type sequence C description BINDING SITE FOR RESIDUE LCY C 202 source : AC6 17) chain C residue 53 type sequence K description BINDING SITE FOR RESIDUE LCY C 202 source : AC6 18) chain D residue 39 type sequence H description BINDING SITE FOR RESIDUE CU D 201 source : AC7 19) chain D residue 89 type sequence C description BINDING SITE FOR RESIDUE CU D 201 source : AC7 20) chain D residue 92 type sequence H description BINDING SITE FOR RESIDUE CU D 201 source : AC7 21) chain D residue 97 type sequence M description BINDING SITE FOR RESIDUE CU D 201 source : AC7 22) chain D residue 45 type sequence C description BINDING SITE FOR RESIDUE LCY D 202 source : AC8 23) chain A residue 39 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 89 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 92 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 97 type BINDING sequence M description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 39 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 89 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 92 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 97 type BINDING sequence M description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 89 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 92 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 97 type BINDING sequence M description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 39 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 89 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 92 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 97 type BINDING sequence M description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 39 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10089349 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 82-97 type prosite sequence AGTYTYYCAPHRGAGM description COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYtYYCa.P.HrgagM source prosite : PS00196

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