4ZE8

PBP AccA from A. tumefaciens C58

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SBP_bac_5_1st	e4ze8A2	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
A	SBP_bac_5_3rd	e4ze8A3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
A	SBP_bac_5_2nd	e4ze8A1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)
B	SBP_bac_5_1st	e4ze8B2	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
B	SBP_bac_5_3rd	e4ze8B1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
B	SBP_bac_5_2nd	e4ze8B3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)
C	SBP_bac_5_1st	e4ze8C1	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
C	SBP_bac_5_3rd	e4ze8C2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
C	SBP_bac_5_2nd	e4ze8C3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)
D	SBP_bac_5_1st	e4ze8D1	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
D	SBP_bac_5_3rd	e4ze8D2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
D	SBP_bac_5_2nd	e4ze8D3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
A	3.90.76.10	Alpha Beta	Alpha-Beta Complex	Dipeptide-binding Protein	domain 1	CATH (4.3.0)
A	3.10.105.10	Alpha Beta	Roll	Dipeptide-binding Protein	domain 3	CATH (4.3.0)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.90.76.10	Alpha Beta	Alpha-Beta Complex	Dipeptide-binding Protein	domain 1	CATH (4.3.0)
B	3.10.105.10	Alpha Beta	Roll	Dipeptide-binding Protein	domain 3	CATH (4.3.0)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.90.76.10	Alpha Beta	Alpha-Beta Complex	Dipeptide-binding Protein	domain 1	CATH (4.3.0)
C	3.10.105.10	Alpha Beta	Roll	Dipeptide-binding Protein	domain 3	CATH (4.3.0)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.90.76.10	Alpha Beta	Alpha-Beta Complex	Dipeptide-binding Protein	domain 1	CATH (4.3.0)
D	3.10.105.10	Alpha Beta	Roll	Dipeptide-binding Protein	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00496	Bacterial extracellular solute-binding proteins, family 5 Middle (SBP_bac_5)	Bacterial extracellular solute-binding proteins, family 5 Middle	The borders of this family are based on the PDBSum definitions of the domain edges for Swiss:P06202.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	ABC transporter, substrate binding protein (Agrocinopines A and B)	peptide transmembrane transporter activity transporter activity transmembrane transporter activity	localization nitrogen compound transport dipeptide transport amide transport transport oligopeptide transport establishment of localization peptide transport	ATPase dependent transmembrane transport complex protein-containing complex plasma membrane protein complex membrane plasma membrane membrane protein complex cellular anatomical entity transporter complex ATP-binding cassette (ABC) transporter complex cell periphery transmembrane transporter complex outer membrane-bounded periplasmic space cell envelope periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000914	Solute-binding protein family 5 domain	Domain
A, B, C, D	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, B, C, D	IPR039424	Solute-binding protein family 5	Family
A, B, C, D	IPR030678	Peptide/nickel binding protein, MppA-type	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.