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2CCY

STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION

Replaces:  1CCY
Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC A 129
ChainResidue
AARG12
ACYS118
ACYS121
AHIS122
ALYS126
AHOH401
AHOH427
BLYS10
AGLN13
AGLN17
ALEU19
ATRP23
AGLU69
ATHR70
APHE82
ATRP86

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC B 129
ChainResidue
ALYS10
BARG12
BGLN13
BMET16
BGLN17
BLEU19
BTRP23
BGLU69
BTHR70
BTRP86
BCYS118
BCYS121
BHIS122
BLYS126
BHOH501
BHOH527

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:3005592, ECO:0007744|PDB:2CCY
ChainResidueDetails
AGLN13
AGLN17
AGLU69
ATHR70
BGLN13
BGLN17
BGLU69
BTHR70

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:3005592, ECO:0007744|PDB:2CCY
ChainResidueDetails
ACYS118
ACYS121
BCYS118
BCYS121

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:3005592, ECO:0007744|PDB:2CCY
ChainResidueDetails
AHIS122
BHIS122

226707

PDB entries from 2024-10-30

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