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5ZYR

Crystal structure of the reductase (C1) component of p-hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
A0036382molecular_functionflavin reductase (NADH) activity
A0042602molecular_functionriboflavin reductase (NADPH) activity
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
B0036382molecular_functionflavin reductase (NADH) activity
B0042602molecular_functionriboflavin reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue FMN A 401
ChainResidue
AVAL45
ASER69
ASER70
APHE96
AALA97
AARG99
ALYS103
APRO245
AARG247
AHOH540
ATHR46
AALA47
AASN48
ASER49
ASER63
AILE64
AASP65
ASER68

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 402
ChainResidue
ATHR218
AARG222
AHOH501
AHOH514
AHOH520
BPRO169
BHIS170

site_idAC3
Number of Residues18
Detailsbinding site for residue FMN B 401
ChainResidue
BVAL45
BTHR46
BALA47
BASN48
BSER49
BSER63
BILE64
BASP65
BSER68
BSER69
BSER70
BPHE96
BALA97
BARG99
BLYS103
BPRO245
BARG247
BHOH524

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT B 402
ChainResidue
APRO169
AHIS170
BTHR218
BARG222
BHOH503

250835

PDB entries from 2026-03-18

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