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2DGE

Crystal structure of oxidized cytochrome C6A from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
C0005506molecular_functioniron ion binding
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
D0005506molecular_functioniron ion binding
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AASP74
AGLU159
CASP74
CLYS155
CGLU159

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 1002
ChainResidue
DGLU159
BASP74
BGLU159
DASP74
DLYS155

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ACYS86
ACYS89
AHIS90
AASN95
AALA101
ATHR102
ALEU103
AASP107
ALEU108
AASN111
ATHR123
ALYS127
AMET130
AHOH1005
AHOH1010
AHOH1025

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BALA85
BCYS86
BCYS89
BHIS90
BASN95
BILE97
BGLN98
BALA101
BTHR102
BLEU103
BASP107
BLEU108
BASN111
BVAL113
BTHR123
BLYS127
BMET130
BPHE133
BHOH1009
BHOH1020

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM C 200
ChainResidue
AARG110
AHOH1002
CALA85
CCYS86
CCYS89
CHIS90
CASN95
CALA101
CTHR102
CLEU103
CASP107
CLEU108
CASN111
CVAL113
CTHR123
CLYS127
CMET130
CPHE133
CHOH223
DGLY88
DILE96

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM D 200
ChainResidue
BARG110
BHOH1012
BHOH1038
CILE96
DALA85
DCYS86
DCYS89
DHIS90
DASN95
DALA101
DTHR102
DLEU103
DASP107
DLEU108
DASN111
DVAL113
DTHR123
DLYS127
DMET130
DPHE133
DHOH207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:16777100, ECO:0000269|PubMed:16815443, ECO:0000269|PubMed:17625855
ChainResidueDetails
ACYS86
ACYS89
BCYS86
BCYS89
CCYS86
CCYS89
DCYS86
DCYS89

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS90
AMET130
BHIS90
BMET130
CHIS90
CMET130
DHIS90
DMET130

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLN98
BGLN98
CGLN98
DGLN98

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PDB entries from 2025-06-11

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