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6DYI

Co(II)-bound structure of the engineered cyt cb562 variant, H3

Functional Information from GO Data
ChainGOidnamespacecontents
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 Residues6
Detailsbinding site for residue CO B 201
ChainResidue
BHIS67
BHIS71
BHIS97
BHOH319
BHOH341
BHOH354

site_idAC2
Number of Residues16
Detailsbinding site for residue HEC B 202
ChainResidue
BASN11
BPRO45
BPRO46
BPHE61
BPHE65
BCYS98
BCYS101
BHIS102
BTYR105
BARG106
BCA206
BHOH314
BHOH325
BGLU4
BMET7
BLEU10

site_idAC3
Number of Residues6
Detailsbinding site for residue CL B 203
ChainResidue
BVAL84
BVAL84
BLYS85
BLYS85
BHOH355
BHOH355

site_idAC4
Number of Residues8
Detailsbinding site for residue CA B 204
ChainResidue
BLYS19
BLYS19
BASP21
BASP21
BHOH350
BHOH350
BHOH357
BHOH357

site_idAC5
Number of Residues3
Detailsbinding site for residue CA B 205
ChainResidue
BASP2
BASP5
BHOH317

site_idAC6
Number of Residues2
Detailsbinding site for residue CA B 206
ChainResidue
BGLU4
BHEC202

site_idAC7
Number of Residues4
Detailsbinding site for residue CA B 207
ChainResidue
BGLU4
BASP5
BGLU8
BHOH312

site_idAC8
Number of Residues8
Detailsbinding site for residue CA B 208
ChainResidue
BGLU81
BGLU81
BGLU81
BGLU81
BHOH326
BHOH326
BHOH326
BHOH326

site_idAC9
Number of Residues3
Detailsbinding site for residue CA B 209
ChainResidue
BALA1
BASP39
BHOH348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
BMET7
BHIS102

223166

PDB entries from 2024-07-31

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